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[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","G0LD09",54.5,3.399999999999999E-147,"ugd KPR_11496 NCTC5046_05057",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB01713","Udp-Alpha-D-Xylopyranose","experimental","unknown"]
[1.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","G0LD09",54.5,3.399999999999999E-147,"ugd KPR_11496 NCTC5046_05057",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB03041","UDP-alpha-D-glucuronic acid","experimental","unknown"]
[2.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A0A377ZCW7",54.5,6.899999999999998E-147,"ugd NCTC5050_01747",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB01713","Udp-Alpha-D-Xylopyranose","experimental","unknown"]
[3.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A0A377ZCW7",54.5,6.899999999999998E-147,"ugd NCTC5050_01747",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB03041","UDP-alpha-D-glucuronic acid","experimental","unknown"]
[4.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A6TBE0",54.5,6.899999999999998E-147,"ugd KPN_02493",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB01713","Udp-Alpha-D-Xylopyranose","experimental","unknown"]
[5.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A6TBE0",54.5,6.899999999999998E-147,"ugd KPN_02493",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB03041","UDP-alpha-D-glucuronic acid","experimental","unknown"]
[6.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A0A0H3GV84",54.5,6.899999999999998E-147,"KPHS_35540",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB01713","Udp-Alpha-D-Xylopyranose","experimental","unknown"]
[7.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A0A0H3GV84",54.5,6.899999999999998E-147,"KPHS_35540",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB03041","UDP-alpha-D-glucuronic acid","experimental","unknown"]
[8.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A378EC02",90.7,0.0,"hisD_1 NCTC5046_05089","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|RuleBase:RU000580}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|RuleBase:RU000580};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[9.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A378EC02",90.7,0.0,"hisD_1 NCTC5046_05089","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|RuleBase:RU000580}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|RuleBase:RU000580};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[10.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A378EC02",90.7,0.0,"hisD_1 NCTC5046_05089","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|RuleBase:RU000580}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|RuleBase:RU000580};",null,"DB09462","Glycerin","approved, investigational","unknown"]
[11.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A378EC02",90.7,0.0,"hisD_1 NCTC5046_05089","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|RuleBase:RU000580}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|RuleBase:RU000580};",null,"DB03811","Histidinol","experimental","unknown"]
[12.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A377ZBQ0",88.4,0.0,"hisD_2 hisD NCTC5050_01774","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[13.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A377ZBQ0",88.4,0.0,"hisD_2 hisD NCTC5050_01774","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[14.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A377ZBQ0",88.4,0.0,"hisD_2 hisD NCTC5050_01774","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB09462","Glycerin","approved, investigational","unknown"]
[15.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A377ZBQ0",88.4,0.0,"hisD_2 hisD NCTC5050_01774","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03811","Histidinol","experimental","unknown"]
[16.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A6TBC3",88.5,0.0,"hisD KPN_02476","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[17.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A6TBC3",88.5,0.0,"hisD KPN_02476","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[18.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A6TBC3",88.5,0.0,"hisD KPN_02476","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB09462","Glycerin","approved, investigational","unknown"]
[19.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A6TBC3",88.5,0.0,"hisD KPN_02476","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03811","Histidinol","experimental","unknown"]
[20.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A0H3GQM4",88.2,0.0,"hisD KPHS_35370","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[21.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A0H3GQM4",88.2,0.0,"hisD KPHS_35370","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[22.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A0H3GQM4",88.2,0.0,"hisD KPHS_35370","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB09462","Glycerin","approved, investigational","unknown"]
[23.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A0H3GQM4",88.2,0.0,"hisD KPHS_35370","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03811","Histidinol","experimental","unknown"]
[24.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A6T4H8",92.3,1.8999999999999994E-177,"dapB KPN78578_00380 KPN_00039","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[25.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A6T4H8",92.3,1.8999999999999994E-177,"dapB KPN78578_00380 KPN_00039","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[26.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A0H3GN28",92.3,1.8999999999999994E-177,"dapB KPHS_07490","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[27.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A0H3GN28",92.3,1.8999999999999994E-177,"dapB KPHS_07490","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[28.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A378C3R8",92.3,1.8999999999999994E-177,"dapB NCTC5050_06692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[29.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A378C3R8",92.3,1.8999999999999994E-177,"dapB NCTC5050_06692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[30.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A378E9V1",91.6,5.199999999999998E-175,"dapB NCTC5046_04201","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[31.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A378E9V1",91.6,5.199999999999998E-175,"dapB NCTC5046_04201","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[32.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A0H3H447",73.4,0.0,"asd KPHS_49510","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[33.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A0H3H447",73.4,0.0,"asd KPHS_49510","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[34.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A0H3H447",73.4,0.0,"asd KPHS_49510","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB04498","Aspartate Semialdehyde","experimental","unknown"]
[35.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378AP86",70.9,1.0999999999999999E-179,"asd_1 asd NCTC5050_02692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[36.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378AP86",70.9,1.0999999999999999E-179,"asd_1 asd NCTC5050_02692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[37.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378AP86",70.9,1.0999999999999999E-179,"asd_1 asd NCTC5050_02692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB04498","Aspartate Semialdehyde","experimental","unknown"]
[38.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A6TF52",73.4,0.0,"asd KPN_03799","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[39.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A6TF52",73.4,0.0,"asd KPN_03799","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[40.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A6TF52",73.4,0.0,"asd KPN_03799","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB04498","Aspartate Semialdehyde","experimental","unknown"]
[41.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378E6L7",73.4,0.0,"asd NCTC5046_02977","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[42.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378E6L7",73.4,0.0,"asd NCTC5046_02977","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[43.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378E6L7",73.4,0.0,"asd NCTC5046_02977","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB04498","Aspartate Semialdehyde","experimental","unknown"]
[44.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A0A378E7A2",78.4,0.0,"murB NCTC5046_02664","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[45.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A0A378E7A2",78.4,0.0,"murB NCTC5046_02664","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[46.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A6TGM9",78.7,0.0,"murB KPN_04350","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[47.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A6TGM9",78.7,0.0,"murB KPN_04350","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[48.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A0A0H3GPZ2",78.7,0.0,"murB KPHS_01910","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[49.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A0A0H3GPZ2",78.7,0.0,"murB KPHS_01910","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[50.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A6TD48",93.7,0.0,"cysI KPN78578_30580 KPN_03118","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. {ECO:0000255|HAMAP-Rule:MF_01540}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01540};",null,"DB02832","Siroheme","experimental","unknown"]
[51.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A0A377Z6G5",97.4,0.0,"cysI_1 NCTC5050_00849",{"$nulls":4},"DB02832","Siroheme","experimental","unknown"]
[52.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A0A377Z5D9",89.3,0.0,"cysI_2 NCTC5050_00850","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. {ECO:0000256|SAAS:SAAS00081128}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01116127};",null,"DB02832","Siroheme","experimental","unknown"]
[53.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A0A378DJI4",94.9,0.0,"cysI_2 NCTC5046_01659",{"$nulls":4},"DB02832","Siroheme","experimental","unknown"]
[54.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A0A0H3GXH1",93.5,0.0,"cysI KPHS_41930","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. {ECO:0000256|HAMAP-Rule:MF_01540, ECO:0000256|SAAS:SAAS00081128}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01540, ECO:0000256|SAAS:SAAS01116127};",null,"DB02832","Siroheme","experimental","unknown"]
[55.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A6TD49",90.3,0.0,"cysJ KPN78578_30590 KPN_03119","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000255|HAMAP-Rule:MF_01541}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01541};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[56.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A6TD49",90.3,0.0,"cysJ KPN78578_30590 KPN_03119","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000255|HAMAP-Rule:MF_01541}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01541};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[57.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A0H3GWU1",90.3,0.0,"cysJ KPHS_41940","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS01115428};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[58.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A0H3GWU1",90.3,0.0,"cysJ KPHS_41940","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS01115428};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[59.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A377Z696",90.2,0.0,"cysJ NCTC5050_00848",{"$nulls":4},"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[60.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A377Z696",90.2,0.0,"cysJ NCTC5050_00848",{"$nulls":4},"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[61.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A378DJ97",91.1,0.0,"cysJ NCTC5046_01660","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01115428};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[62.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A378DJ97",91.1,0.0,"cysJ NCTC5046_01660","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01115428};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[63.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[64.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[65.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[66.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[67.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[68.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[69.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[70.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[71.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[72.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[73.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[74.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[75.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[76.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[77.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[78.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[79.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[80.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[81.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[82.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[83.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[84.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[85.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[86.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[87.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[88.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03038","LY341770","experimental","unknown"]
[89.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[90.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[91.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[92.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[93.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03558","Sp-876","experimental","unknown"]
[94.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[95.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[96.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[97.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[98.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[99.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[100.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[101.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04503","Sp-722","experimental","unknown"]
[102.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[103.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04586","2-bromophenol","experimental","unknown"]
[104.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[105.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[106.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[107.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[108.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[109.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[110.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03038","LY341770","experimental","unknown"]
[111.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[112.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[113.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[114.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[115.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03558","Sp-876","experimental","unknown"]
[116.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[117.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[118.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[119.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[120.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[121.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[122.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[123.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04503","Sp-722","experimental","unknown"]
[124.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[125.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04586","2-bromophenol","experimental","unknown"]
[126.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[127.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[128.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[129.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Shigella flexneri","P0A789","BE0001928","A0A0H3GMI1",93.9,0.0,"pyrB KPHS_05040","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00001};",null,"DB03459","Sparfosic acid","experimental","unknown"]
[130.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Shigella flexneri","P0A789","BE0001928","A0A378B0J6",93.9,0.0,"pyrB NCTC5050_03825","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00001};",null,"DB03459","Sparfosic acid","experimental","unknown"]
[131.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Shigella flexneri","P0A789","BE0001928","A6THH4",93.9,0.0,"pyrB KPN78578_45840 KPN_04657","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00001};",null,"DB03459","Sparfosic acid","experimental","unknown"]
[132.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Escherichia coli (strain K12)","P0A786","BE0003341","A0A0H3GMI1",93.9,0.0,"pyrB KPHS_05040","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00001};",null,"DB05540","Alanosine","investigational","unknown"]
[133.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Escherichia coli (strain K12)","P0A786","BE0003341","A0A378B0J6",93.9,0.0,"pyrB NCTC5050_03825","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00001};",null,"DB05540","Alanosine","investigational","unknown"]
[134.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Escherichia coli (strain K12)","P0A786","BE0003341","A6THH4",93.9,0.0,"pyrB KPN78578_45840 KPN_04657","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00001};",null,"DB05540","Alanosine","investigational","unknown"]
[135.0,"2.1.3.3","Ornithine carbamoyltransferase chain I","Escherichia coli (strain K12)","P04391","BE0001875","A0A0H3GHJ1",88.9,0.0,"KPHS_05120",null,"FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. {ECO:0000256|SAAS:SAAS00009102}.","CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|SAAS:SAAS01125822};",null,"DB02965","Ndelta-(N'-Sulphodiaminophosphinyl)-L-Ornithine","experimental","unknown"]
[136.0,"2.1.3.3","Ornithine carbamoyltransferase chain I","Escherichia coli (strain K12)","P04391","BE0001875","A6THH6",89.2,0.0,"argI KPN_04659","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3. ","FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. {ECO:0000256|SAAS:SAAS00009102}.","CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|SAAS:SAAS01125822};",null,"DB02965","Ndelta-(N'-Sulphodiaminophosphinyl)-L-Ornithine","experimental","unknown"]
[137.0,"2.1.3.3","Ornithine carbamoyltransferase chain I","Escherichia coli (strain K12)","P04391","BE0001875","A0A378B121",89.2,0.0,"argI NCTC5050_03827",null,"FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. {ECO:0000256|SAAS:SAAS00009102}.","CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|SAAS:SAAS01125822};",null,"DB02965","Ndelta-(N'-Sulphodiaminophosphinyl)-L-Ornithine","experimental","unknown"]
[138.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[139.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03134","2-Aminopimelic Acid","experimental","unknown"]
[140.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01856","Pimelic Acid","experimental","unknown"]
[141.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03699","Succinyl-Coenzyme A","experimental","unknown"]
[142.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03905","Succinamide-Coa","experimental","unknown"]
[143.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[144.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03134","2-Aminopimelic Acid","experimental","unknown"]
[145.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01856","Pimelic Acid","experimental","unknown"]
[146.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03699","Succinyl-Coenzyme A","experimental","unknown"]
[147.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03905","Succinamide-Coa","experimental","unknown"]
[148.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[149.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03134","2-Aminopimelic Acid","experimental","unknown"]
[150.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01856","Pimelic Acid","experimental","unknown"]
[151.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03699","Succinyl-Coenzyme A","experimental","unknown"]
[152.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03905","Succinamide-Coa","experimental","unknown"]
[153.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[154.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB03134","2-Aminopimelic Acid","experimental","unknown"]
[155.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB01856","Pimelic Acid","experimental","unknown"]
[156.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB03699","Succinyl-Coenzyme A","experimental","unknown"]
[157.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB03905","Succinamide-Coa","experimental","unknown"]
[158.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A0H3GMW8",42.4,5.4000000000000005E-58,"lpxA KPHS_09280","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[159.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A0H3GMW8",42.4,5.4000000000000005E-58,"lpxA KPHS_09280","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[160.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A6T4Y3",42.4,5.4000000000000005E-58,"lpxA KPN78578_01930 KPN_00194","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-Rule:MF_00387};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[161.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A6T4Y3",42.4,5.4000000000000005E-58,"lpxA KPN78578_01930 KPN_00194","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-Rule:MF_00387};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[162.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A378C0J0",42.4,2.7000000000000002E-58,"lpxA NCTC10313_01586 NCTC5050_06478","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[163.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A378C0J0",42.4,2.7000000000000002E-58,"lpxA NCTC10313_01586 NCTC5050_06478","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[164.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A378EC06",42.4,2.7000000000000002E-58,"lpxA NCTC5046_04408","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[165.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A378EC06",42.4,2.7000000000000002E-58,"lpxA NCTC5046_04408","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[166.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB09414","Dipotassium phosphate","approved","unknown"]
[167.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08407","PLATENSIMYCIN","experimental","unknown"]
[168.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB03017","Lauric Acid","approved, experimental","unknown"]
[169.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB01034","Cerulenin","approved","yes","inhibitor"]
[170.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08366","3-({3-[(1S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxodecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid","experimental","unknown"]
[171.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB09414","Dipotassium phosphate","approved","unknown"]
[172.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08407","PLATENSIMYCIN","experimental","unknown"]
[173.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB03017","Lauric Acid","approved, experimental","unknown"]
[174.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB01034","Cerulenin","approved","yes","inhibitor"]
[175.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08366","3-({3-[(1S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxodecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid","experimental","unknown"]
[176.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB09414","Dipotassium phosphate","approved","unknown"]
[177.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08407","PLATENSIMYCIN","experimental","unknown"]
[178.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB03017","Lauric Acid","approved, experimental","unknown"]
[179.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB01034","Cerulenin","approved","yes","inhibitor"]
[180.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08366","3-({3-[(1S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxodecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid","experimental","unknown"]
[181.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[182.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[183.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[184.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[185.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[186.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[187.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[188.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[189.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[190.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[191.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[192.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[193.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[194.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[195.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[196.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[197.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[198.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[199.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[200.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[201.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[202.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[203.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[204.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[205.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[206.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[207.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[208.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[209.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[210.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[211.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[212.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[213.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","A6T4N3",89.6,0.0,"murG KPN78578_00930 KPN_00094","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[214.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","A0A0H3GJ97",89.6,0.0,"murG KPHS_08100","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00765558}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS01124123};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[215.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","A0A378EBK5",88.7,1.7999999999999995E-147,"murG_2 NCTC5046_04271","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000256|SAAS:SAAS00765558}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000256|SAAS:SAAS01124123};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[216.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","A0A378C1B0",88.1,1.5999999999999996E-144,"murG_1 NCTC5050_06619","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000256|SAAS:SAAS00765558}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000256|SAAS:SAAS01124123};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[217.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A0H3GXD7",93.4,1.1999999999999995E-139,"pyrE KPHS_51450","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[218.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A0H3GXD7",93.4,1.1999999999999995E-139,"pyrE KPHS_51450","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[219.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A6TFN4",93.9,1.3999999999999994E-140,"pyrE KPN78578_39440 KPN_03983","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[220.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A6TFN4",93.9,1.3999999999999994E-140,"pyrE KPN78578_39440 KPN_03983","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[221.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A378AUX2",90.1,2.2999999999999992E-77,"pyrE NCTC5050_03219","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[222.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A378AUX2",90.1,2.2999999999999992E-77,"pyrE NCTC5050_03219","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[223.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A378E7H8",93.9,8.1999999999999975E-140,"pyrE NCTC5046_02750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[224.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A378E7H8",93.9,8.1999999999999975E-140,"pyrE NCTC5046_02750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[225.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A6TBZ8",96.6,0.0,"purF KPN_02702","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[226.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A6TBZ8",96.6,0.0,"purF KPN_02702","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[227.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A6TBZ8",96.6,0.0,"purF KPN_02702","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[228.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A378CQK2",96.6,0.0,"purF NCTC5046_00589","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[229.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A378CQK2",96.6,0.0,"purF NCTC5046_00589","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[230.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A378CQK2",96.6,0.0,"purF NCTC5046_00589","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[231.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A377Z9V1",96.6,0.0,"purF NCTC10313_04977 NCTC5050_01433","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[232.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A377Z9V1",96.6,0.0,"purF NCTC10313_04977 NCTC5050_01433","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[233.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A377Z9V1",96.6,0.0,"purF NCTC10313_04977 NCTC5050_01433","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[234.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A0H3H133",96.6,0.0,"purF KPHS_37710","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[235.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A0H3H133",96.6,0.0,"purF KPHS_37710","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[236.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A0H3H133",96.6,0.0,"purF KPHS_37710","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[237.0,"2.4.2.17","ATP phosphoribosyltransferase","Escherichia coli (strain K12)","P60757","BE0001228","A0A377ZDD3",94.0,0.0,"hisG NCTC10313_04649 NCTC5050_01775","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. ","FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. {ECO:0000256|HAMAP-Rule:MF_00079}.","CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17; Evidence={ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS01121154};",null,"DB01661","Phosphoribosyl Atp","experimental","unknown"]
[238.0,"2.4.2.17","ATP phosphoribosyltransferase","Escherichia coli (strain K12)","P60757","BE0001228","A6TBC2",94.0,0.0,"hisG KPN78578_24320 KPN_02475","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. ","FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. {ECO:0000255|HAMAP-Rule:MF_00079}.","CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00079};",null,"DB01661","Phosphoribosyl Atp","experimental","unknown"]
[239.0,"2.4.2.17","ATP phosphoribosyltransferase","Escherichia coli (strain K12)","P60757","BE0001228","A0A378EE61",93.8,4.6999999999999986E-114,"hisG_2 NCTC5046_05092","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. ","FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. {ECO:0000256|SAAS:SAAS00046314}.","CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17; Evidence={ECO:0000256|SAAS:SAAS01121154};",null,"DB01661","Phosphoribosyl Atp","experimental","unknown"]
[240.0,"2.4.2.17","ATP phosphoribosyltransferase","Escherichia coli (strain K12)","P60757","BE0001228","A0A0H3H0I5",94.0,0.0,"hisG KPHS_35360","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. ","FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. {ECO:0000256|HAMAP-Rule:MF_00079}.","CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17; Evidence={ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS01121154};",null,"DB01661","Phosphoribosyl Atp","experimental","unknown"]
[241.0,"2.4.2.18","Anthranilate phosphoribosyltransferase","Erwinia carotovora","Q8VP84","BE0002489","A6T7W8",73.1,6.399999999999999E-169,"trpD KPN_01256","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. ","FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS00918330}.","CATALYTIC ACTIVITY: Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18; Evidence={ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01124167};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[242.0,"2.4.2.18","Anthranilate phosphoribosyltransferase","Erwinia carotovora","Q8VP84","BE0002489","A0A0H3GLX6",73.1,6.399999999999999E-169,"trpD KPHS_21620","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. ","FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS00918330}.","CATALYTIC ACTIVITY: Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18; Evidence={ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01124167};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[243.0,"2.4.2.18","Anthranilate phosphoribosyltransferase","Erwinia carotovora","Q8VP84","BE0002489","A0A378EHA3",72.8,2.5999999999999996E-168,"trpD NCTC5046_07037","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. ","FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS00918330}.","CATALYTIC ACTIVITY: Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18; Evidence={ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01124167};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[244.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378BNF7",88.7,5.4E-174,"aroA_2 NCTC5050_05393","Metabolic intermediate biosynthesis; chorismate biosynthesis. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|SAAS:SAAS01118199};",null,"DB03116","5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate","experimental","unknown"]
[245.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378BNF7",88.7,5.4E-174,"aroA_2 NCTC5050_05393","Metabolic intermediate biosynthesis; chorismate biosynthesis. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|SAAS:SAAS01118199};",null,"DB01942","Formic Acid","approved, experimental","unknown"]
[246.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378BNF7",88.7,5.4E-174,"aroA_2 NCTC5050_05393","Metabolic intermediate biosynthesis; chorismate biosynthesis. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown"]
[247.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378BNF7",88.7,5.4E-174,"aroA_2 NCTC5050_05393","Metabolic intermediate biosynthesis; chorismate biosynthesis. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[248.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A6T701",89.0,0.0,"aroA KPN78578_09110 KPN_00936","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00210};",null,"DB03116","5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate","experimental","unknown"]
[249.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A6T701",89.0,0.0,"aroA KPN78578_09110 KPN_00936","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00210};",null,"DB01942","Formic Acid","approved, experimental","unknown"]
[250.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A6T701",89.0,0.0,"aroA KPN78578_09110 KPN_00936","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00210};",null,"DB04539","Glyphosate","experimental","unknown"]
[251.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A6T701",89.0,0.0,"aroA KPN78578_09110 KPN_00936","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00210};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[252.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378DHG0",89.0,0.0,"aroA NCTC5046_01000","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB03116","5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate","experimental","unknown"]
[253.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378DHG0",89.0,0.0,"aroA NCTC5046_01000","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB01942","Formic Acid","approved, experimental","unknown"]
[254.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378DHG0",89.0,0.0,"aroA NCTC5046_01000","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown"]
[255.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378DHG0",89.0,0.0,"aroA NCTC5046_01000","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[256.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A0H3GV01",89.2,0.0,"aroA KPHS_18160","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB03116","5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate","experimental","unknown"]
[257.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A0H3GV01",89.2,0.0,"aroA KPHS_18160","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB01942","Formic Acid","approved, experimental","unknown"]
[258.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A0H3GV01",89.2,0.0,"aroA KPHS_18160","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown"]
[259.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A0H3GV01",89.2,0.0,"aroA KPHS_18160","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[260.0,"2.5.1.48","Cystathionine gamma-synthase","Escherichia coli (strain K12)","P00935","BE0003209","A0A378E8P3",95.8,0.0,"metB NCTC5046_03255",{"$nulls":4},"DB04083","N'-Pyridoxyl-Lysine-5'-Monophosphate","experimental","unknown"]
[261.0,"2.5.1.48","Cystathionine gamma-synthase","Escherichia coli (strain K12)","P00935","BE0003209","A0A0H3GPP8",95.8,0.0,"KPHS_00860",{"$nulls":4},"DB04083","N'-Pyridoxyl-Lysine-5'-Monophosphate","experimental","unknown"]
[262.0,"2.5.1.48","Cystathionine gamma-synthase","Escherichia coli (strain K12)","P00935","BE0003209","A0A378AUN9",95.8,0.0,"metB NCTC10313_07038 NCTC5050_03330",{"$nulls":4},"DB04083","N'-Pyridoxyl-Lysine-5'-Monophosphate","experimental","unknown"]
[263.0,"2.5.1.48","Cystathionine gamma-synthase","Escherichia coli (strain K12)","P00935","BE0003209","A6TGC8",95.8,0.0,"metB KPN_04233",{"$nulls":4},"DB04083","N'-Pyridoxyl-Lysine-5'-Monophosphate","experimental","unknown"]
[264.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A0H3GUB6",95.4,0.0,"kdsA KPHS_32290","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB01819","Phosphoenolpyruvate","experimental","unknown"]
[265.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A0H3GUB6",95.4,0.0,"kdsA KPHS_32290","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[266.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A0H3GUB6",95.4,0.0,"kdsA KPHS_32290","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[267.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A0H3GUB6",95.4,0.0,"kdsA KPHS_32290","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[268.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378EE77",95.4,0.0,"kdsA NCTC5046_05810","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB01819","Phosphoenolpyruvate","experimental","unknown"]
[269.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378EE77",95.4,0.0,"kdsA NCTC5046_05810","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[270.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378EE77",95.4,0.0,"kdsA NCTC5046_05810","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[271.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378EE77",95.4,0.0,"kdsA NCTC5046_05810","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[272.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378BC15",95.4,0.0,"kdsA NCTC5050_04802","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB01819","Phosphoenolpyruvate","experimental","unknown"]
[273.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378BC15",95.4,0.0,"kdsA NCTC5050_04802","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[274.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378BC15",95.4,0.0,"kdsA NCTC5050_04802","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[275.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378BC15",95.4,0.0,"kdsA NCTC5050_04802","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[276.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A6TAN5",95.4,0.0,"kdsA KPN78578_21950 KPN_02230","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000255|HAMAP-Rule:MF_00056};",null,"DB01819","Phosphoenolpyruvate","experimental","unknown"]
[277.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A6TAN5",95.4,0.0,"kdsA KPN78578_21950 KPN_02230","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000255|HAMAP-Rule:MF_00056};",null,"DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[278.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A6TAN5",95.4,0.0,"kdsA KPN78578_21950 KPN_02230","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000255|HAMAP-Rule:MF_00056};",null,"DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[279.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A6TAN5",95.4,0.0,"kdsA KPN78578_21950 KPN_02230","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000255|HAMAP-Rule:MF_00056};",null,"DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[280.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[281.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[282.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[283.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[284.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[285.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[286.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[287.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[288.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[289.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[290.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[291.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[292.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[293.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[294.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[295.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[296.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[297.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[298.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[299.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[300.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","A6TEK8",92.1,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[301.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","A0A378E6U7",92.4,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[302.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","A0A0H3GYZ6",92.1,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[303.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","A0A378AHV3",92.1,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[304.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","A0A378E6U7",92.4,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[305.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","A0A0H3GYZ6",92.1,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[306.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","A0A378AHV3",92.1,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[307.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","A6TEK8",92.1,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[308.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[309.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[310.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[311.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[312.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[313.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[314.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[315.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[316.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[317.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[318.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[319.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[320.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[321.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[322.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[323.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[324.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[325.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[326.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[327.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[328.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[329.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[330.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[331.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[332.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A0H3GPS2",94.8,0.0,"ilvE KPHS_01160","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[333.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A0H3GPS2",94.8,0.0,"ilvE KPHS_01160","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03553","Glutaric Acid","experimental","unknown"]
[334.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A0H3GPS2",94.8,0.0,"ilvE KPHS_01160","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03993","4-Methyl Valeric Acid","experimental","unknown"]
[335.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A0H3GPS2",94.8,0.0,"ilvE KPHS_01160","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB04063","2-Methylleucine","experimental","unknown"]
[336.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A6TGF7",94.8,0.0,"ilvE KPN_04269","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[337.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A6TGF7",94.8,0.0,"ilvE KPN_04269","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03553","Glutaric Acid","experimental","unknown"]
[338.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A6TGF7",94.8,0.0,"ilvE KPN_04269","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03993","4-Methyl Valeric Acid","experimental","unknown"]
[339.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A6TGF7",94.8,0.0,"ilvE KPN_04269","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB04063","2-Methylleucine","experimental","unknown"]
[340.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378AS62",94.8,0.0,"ilvE NCTC5050_02940","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[341.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378AS62",94.8,0.0,"ilvE NCTC5050_02940","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03553","Glutaric Acid","experimental","unknown"]
[342.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378AS62",94.8,0.0,"ilvE NCTC5050_02940","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03993","4-Methyl Valeric Acid","experimental","unknown"]
[343.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378AS62",94.8,0.0,"ilvE NCTC5050_02940","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB04063","2-Methylleucine","experimental","unknown"]
[344.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378E787",94.7,2.8999999999999992E-114,"ilvE_1 ilvE NCTC5046_03301","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[345.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378E787",94.7,2.8999999999999992E-114,"ilvE_1 ilvE NCTC5046_03301","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03553","Glutaric Acid","experimental","unknown"]
[346.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378E787",94.7,2.8999999999999992E-114,"ilvE_1 ilvE NCTC5046_03301","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03993","4-Methyl Valeric Acid","experimental","unknown"]
[347.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378E787",94.7,2.8999999999999992E-114,"ilvE_1 ilvE NCTC5046_03301","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB04063","2-Methylleucine","experimental","unknown"]
[348.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A377ZEZ0",85.3,6.499999999999999E-137,"hisC_2 NCTC5050_01772",{"$nulls":4},"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[349.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A377ZEZ0",85.3,6.499999999999999E-137,"hisC_2 NCTC5050_01772",{"$nulls":4},"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[350.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A377ZEZ0",85.3,6.499999999999999E-137,"hisC_2 NCTC5050_01772",{"$nulls":4},"DB03997","L-histidinol phosphate","experimental","unknown"]
[351.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A0H3GVS5",84.1,0.0,"hisC KPHS_35380","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[352.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A0H3GVS5",84.1,0.0,"hisC KPHS_35380","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[353.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A0H3GVS5",84.1,0.0,"hisC KPHS_35380","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB03997","L-histidinol phosphate","experimental","unknown"]
[354.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A378EDY0",84.1,0.0,"hisC NCTC5046_05088","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[355.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A378EDY0",84.1,0.0,"hisC NCTC5046_05088","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[356.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A378EDY0",84.1,0.0,"hisC NCTC5046_05088","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB03997","L-histidinol phosphate","experimental","unknown"]
[357.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A6TBC4",84.4,0.0,"hisC KPN78578_24340 KPN_02477","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[358.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A6TBC4",84.4,0.0,"hisC KPN78578_24340 KPN_02477","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[359.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A6TBC4",84.4,0.0,"hisC KPN78578_24340 KPN_02477","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB03997","L-histidinol phosphate","experimental","unknown"]
[360.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E8W0",93.8,5.9E-43,"argB_2 NCTC5046_03277",{"$nulls":4},"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[361.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E8W0",93.8,5.9E-43,"argB_2 NCTC5046_03277",{"$nulls":4},"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[362.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E8W0",93.8,5.9E-43,"argB_2 NCTC5046_03277",{"$nulls":4},"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[363.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E7A4",91.9,3.9999999999999993E-106,"argB_1 NCTC5046_03276","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|SAAS:SAAS01124576};",null,"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[364.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E7A4",91.9,3.9999999999999993E-106,"argB_1 NCTC5046_03276","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|SAAS:SAAS01124576};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[365.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E7A4",91.9,3.9999999999999993E-106,"argB_1 NCTC5046_03276","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|SAAS:SAAS01124576};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[366.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A6TGE3",93.0,3.2999999999999996E-166,"argB KPN78578_42030 KPN_04248","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00082};",null,"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[367.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A6TGE3",93.0,3.2999999999999996E-166,"argB KPN78578_42030 KPN_04248","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00082};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[368.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A6TGE3",93.0,3.2999999999999996E-166,"argB KPN78578_42030 KPN_04248","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00082};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[369.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A0H3GPQ8",93.0,1.2999999999999998E-165,"argB KPHS_01010","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[370.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A0H3GPQ8",93.0,1.2999999999999998E-165,"argB KPHS_01010","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[371.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A0H3GPQ8",93.0,1.2999999999999998E-165,"argB KPHS_01010","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[372.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378AUU7",92.6,2.9999999999999985E-164,"argB NCTC5050_03349","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[373.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378AUU7",92.6,2.9999999999999985E-164,"argB NCTC5050_03349","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[374.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378AUU7",92.6,2.9999999999999985E-164,"argB NCTC5050_03349","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[375.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","A6T7F8",84.3,1.4999999999999995E-119,"tmk KPN78578_10680 KPN_01096",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000255|HAMAP-Rule:MF_00165}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00165};",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[376.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","A0A0H3GMT6",84.3,1.4999999999999995E-119,"tmk KPHS_19750",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-Rule:MF_00165}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[377.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","A0A377ZWF0",84.3,1.4999999999999995E-119,"tmk NCTC10313_04311 NCTC5050_01826",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-Rule:MF_00165}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[378.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","A0A378CRW1",83.8,4.399999999999999E-119,"tmk NCTC5046_00789",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-Rule:MF_00165}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[379.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","A0A378E8H7",68.6,0.0,"glmU NCTC5046_03131","Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083685}.","CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124206}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124218};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[380.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","A0A0H3GVB1",68.9,0.0,"glmU KPHS_53020","Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083685}.","CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124206}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124218};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[381.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","A6TG34",68.6,0.0,"glmU KPN78578_40940 KPN_04135","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[382.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","A0A0H3GTS8",41.7,1.9E-33,"KPHS_47470","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. ","FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[383.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","A0A378AHM5",41.1,5.4E-33,"kdsC NCTC10313_00960 NCTC5050_02446","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. ","FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[384.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","A6TEL7",41.7,1.9E-33,"yrbI KPN_03608","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. ","FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[385.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","A0A378E6Z2",41.7,1.9E-33,"kdsC NCTC5046_02530","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. ","FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[386.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A378CRM0",89.1,0.0,"pyrC_2 pyrC NCTC5046_00750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[387.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A378CRM0",89.1,0.0,"pyrC_2 pyrC NCTC5046_00750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[388.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A378CRM0",89.1,0.0,"pyrC_2 pyrC NCTC5046_00750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[389.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A378CRM0",89.1,0.0,"pyrC_2 pyrC NCTC5046_00750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[390.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A377ZDG2",89.4,0.0,"pyrC NCTC5050_01794","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[391.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A377ZDG2",89.4,0.0,"pyrC NCTC5050_01794","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[392.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A377ZDG2",89.4,0.0,"pyrC NCTC5050_01794","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[393.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A377ZDG2",89.4,0.0,"pyrC NCTC5050_01794","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[394.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A6T7D6",89.7,0.0,"pyrC KPN78578_10460 KPN_01074","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[395.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A6T7D6",89.7,0.0,"pyrC KPN78578_10460 KPN_01074","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[396.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A6T7D6",89.7,0.0,"pyrC KPN78578_10460 KPN_01074","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[397.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A6T7D6",89.7,0.0,"pyrC KPN78578_10460 KPN_01074","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[398.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A378EEI5",87.1,0.0,"lysA NCTC5046_05290","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[399.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A378EEI5",87.1,0.0,"lysA NCTC5046_05290","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03252","D-Lysine","experimental","unknown"]
[400.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A377Z4Z0",87.1,0.0,"lysA lysA_1 NCTC10313_05801 NCTC5050_00670","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[401.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A377Z4Z0",87.1,0.0,"lysA lysA_1 NCTC10313_05801 NCTC5050_00670","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03252","D-Lysine","experimental","unknown"]
[402.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A0H3GSP6",87.1,0.0,"lysA KPHS_43170","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[403.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A0H3GSP6",87.1,0.0,"lysA KPHS_43170","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03252","D-Lysine","experimental","unknown"]
[404.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A6TDH9",87.1,0.0,"lysA KPN_03252","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[405.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A6TDH9",87.1,0.0,"lysA KPN_03252","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03252","D-Lysine","experimental","unknown"]
[406.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A0A377ZGT0",85.3,2.5999999999999992E-145,"pyrF NCTC10313_04086 NCTC5050_02067","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[407.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A0A377ZGT0",85.3,2.5999999999999992E-145,"pyrF NCTC10313_04086 NCTC5050_02067","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[408.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A6T7Y9",85.5,1.3999999999999997E-136,"pyrF KPN_01277","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[409.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A6T7Y9",85.5,1.3999999999999997E-136,"pyrF KPN_01277","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[410.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A0A0H3GNE4",85.5,1.3999999999999997E-136,"pyrF KPHS_21850","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[411.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A0A0H3GNE4",85.5,1.3999999999999997E-136,"pyrF KPHS_21850","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[412.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","A0A378EBZ2",56.1,6.599999999999999E-88,"aroD NCTC5046_04243","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[413.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","A0A0H3GMI6",55.7,1.8999999999999998E-87,"aroD KPHS_07880","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[414.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","A0A378C2N8",55.7,1.8999999999999998E-87,"aroD NCTC5050_06648","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[415.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","A6T4L2",56.1,6.599999999999999E-88,"aroD KPN78578_00720 KPN_00073","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[416.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","A0A378C2N8",31.0,2.6E-25,"aroD NCTC5050_06648","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[417.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","A0A378EBZ2",31.0,2.6E-25,"aroD NCTC5046_04243","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[418.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","A0A0H3GMI6",31.0,2.6E-25,"aroD KPHS_07880","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[419.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","A6T4L2",31.0,2.6E-25,"aroD KPN78578_00720 KPN_00073","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[420.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","A0A378BP67",97.7,9.999999999999999E-123,"fabA NCTC10313_04481 NCTC5050_05321","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[421.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","A0A0H3GL47",97.7,9.999999999999999E-123,"fabA KPHS_18620","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[422.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","A6T748",97.7,9.999999999999999E-123,"fabA KPN78578_09580 KPN_00983","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000255|HAMAP-Rule:MF_00405}.","CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000255|HAMAP-Rule:MF_00405}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000255|HAMAP-Rule:MF_00405}; CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00405};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[423.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","A0A378EC77",97.7,9.999999999999999E-123,"fabA NCTC5046_05152","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[424.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","A6T748",97.7,9.999999999999999E-123,"fabA KPN78578_09580 KPN_00983","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000255|HAMAP-Rule:MF_00405}.","CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000255|HAMAP-Rule:MF_00405}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000255|HAMAP-Rule:MF_00405}; CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00405};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[425.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","A0A378EC77",97.7,9.999999999999999E-123,"fabA NCTC5046_05152","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[426.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","A0A0H3GL47",97.7,9.999999999999999E-123,"fabA KPHS_18620","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[427.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","A0A378BP67",97.7,9.999999999999999E-123,"fabA NCTC10313_04481 NCTC5050_05321","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[428.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","A0A378CQP1",46.4,6.599999999999999E-98,"aroC NCTC5046_00568","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000256|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[429.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","A0A0H3GWE8",46.4,4.599999999999999E-98,"aroC KPHS_37880","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000256|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[430.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","A6TC15",46.4,4.599999999999999E-98,"aroC KPN78578_26750 KPN_02719","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[431.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB03435","Uridine-5'-Diphosphate","experimental","unknown"]
[432.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[433.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB02790","Phenyl-Uridine-5'-Diphosphate","experimental","unknown"]
[434.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB02421","Uridine-5'-Diphosphate-Mannose","experimental","unknown"]
[435.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB04097","Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose","experimental","unknown"]
[436.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB01861","Uridine diphosphate glucose","experimental","unknown"]
[437.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB03435","Uridine-5'-Diphosphate","experimental","unknown"]
[438.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[439.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB02790","Phenyl-Uridine-5'-Diphosphate","experimental","unknown"]
[440.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB02421","Uridine-5'-Diphosphate-Mannose","experimental","unknown"]
[441.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB04097","Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose","experimental","unknown"]
[442.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB01861","Uridine diphosphate glucose","experimental","unknown"]
[443.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB03435","Uridine-5'-Diphosphate","experimental","unknown"]
[444.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[445.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB02790","Phenyl-Uridine-5'-Diphosphate","experimental","unknown"]
[446.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB02421","Uridine-5'-Diphosphate-Mannose","experimental","unknown"]
[447.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB04097","Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose","experimental","unknown"]
[448.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB01861","Uridine diphosphate glucose","experimental","unknown"]
[449.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB03435","Uridine-5'-Diphosphate","experimental","unknown"]
[450.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[451.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB02790","Phenyl-Uridine-5'-Diphosphate","experimental","unknown"]
[452.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB02421","Uridine-5'-Diphosphate-Mannose","experimental","unknown"]
[453.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB04097","Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose","experimental","unknown"]
[454.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB01861","Uridine diphosphate glucose","experimental","unknown"]
[455.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A6TFL4",97.4,0.0,"hldD KPN78578_39240 KPN_03963","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[456.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A6TFL4",97.4,0.0,"hldD KPN78578_39240 KPN_03963","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[457.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A0H3GUR3",97.4,0.0,"hldD KPHS_51220","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[458.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A0H3GUR3",97.4,0.0,"hldD KPHS_51220","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[459.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A377YYC3",97.4,0.0,"hldD NCTC10313_00421 NCTC5050_03246","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[460.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A377YYC3",97.4,0.0,"hldD NCTC10313_00421 NCTC5050_03246","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[461.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A378E7F1",97.4,0.0,"hldD NCTC5046_02773","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[462.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A378E7F1",97.4,0.0,"hldD NCTC5046_02773","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[463.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","A6TEG8",54.9,1.8999999999999996E-70,"diaA KPN78578_35280 KPN_03557",null,"FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. {ECO:0000255|HAMAP-Rule:MF_01157}.",null,null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[464.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","A0A377YYQ4",54.9,1.8999999999999996E-70,"yraO diaA NCTC10313_01032 NCTC5050_02380",null,"FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. {ECO:0000256|HAMAP-Rule:MF_01157, ECO:0000256|SAAS:SAAS00846119}.",null,null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[465.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","A0A0H3GXZ7",54.9,1.8999999999999996E-70,"diaA KPHS_46940",null,"FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. {ECO:0000256|HAMAP-Rule:MF_01157, ECO:0000256|SAAS:SAAS00846119}.",null,null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[466.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","A0A378E6M5",54.9,1.8999999999999996E-70,"yraO diaA NCTC5046_02468",null,"FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. {ECO:0000256|HAMAP-Rule:MF_01157, ECO:0000256|SAAS:SAAS00846119}.",null,null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[467.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A0A377ZAQ0",89.4,0.0,"pheA NCTC5050_01083",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[468.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A6TCK5",89.4,0.0,"pheA KPN_02920",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[469.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A0A0H3GTV9",89.4,0.0,"KPHS_39900",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[470.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A0A378EB22",94.1,3.899999999999999E-72,"pheA_2 NCTC5046_04703",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[471.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A0A378EAY2",88.5,6.699999999999998E-84,"pheA_1 pheA NCTC5046_04702","Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O; Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51; Evidence={ECO:0000256|RuleBase:RU361254};",null,"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[472.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A0H3GJ91",91.7,0.0,"murE KPHS_08050","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[473.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A0H3GJ91",91.7,0.0,"murE KPHS_08050","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[474.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A0H3GJ91",91.7,0.0,"murE KPHS_08050","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[475.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A6T4M8",91.7,0.0,"murE KPN_00089","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[476.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A6T4M8",91.7,0.0,"murE KPN_00089","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[477.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A6T4M8",91.7,0.0,"murE KPN_00089","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[478.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378EC10",91.7,0.0,"murE NCTC5046_04264","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[479.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378EC10",91.7,0.0,"murE NCTC5046_04264","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[480.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378EC10",91.7,0.0,"murE NCTC5046_04264","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[481.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378C1F3",91.9,0.0,"murE NCTC5050_06625","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[482.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378C1F3",91.9,0.0,"murE NCTC5050_06625","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[483.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378C1F3",91.9,0.0,"murE NCTC5050_06625","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[484.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A0A0H3GI71",67.9,0.0,"murC KPHS_08120","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[485.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A0A0H3GI71",67.9,0.0,"murC KPHS_08120","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[486.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A0A0H3GI71",67.9,0.0,"murC KPHS_08120","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[487.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A6T4N4",67.9,0.0,"murC KPN78578_00940 KPN_00095","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[488.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A6T4N4",67.9,0.0,"murC KPN78578_00940 KPN_00095","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[489.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A6T4N4",67.9,0.0,"murC KPN78578_00940 KPN_00095","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[490.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[491.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[492.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[493.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[494.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[495.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[496.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[497.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[498.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[499.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[500.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[501.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[502.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[503.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[504.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[505.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[506.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[507.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[508.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[509.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[510.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[511.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[512.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[513.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[514.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[515.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[516.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[517.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[518.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[519.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[520.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[521.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[522.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[523.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[524.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[525.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[526.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[527.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[528.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[529.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[530.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[531.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[532.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[533.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[534.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[535.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[536.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[537.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[538.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[539.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[540.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[541.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[542.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[543.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[544.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[545.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[546.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[547.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[548.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[549.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[550.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[551.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[552.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[553.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[554.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[555.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[556.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[557.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[558.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[559.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[560.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[561.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[562.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[563.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[564.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[565.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[566.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A6TH93",95.4,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[567.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A6TH93",95.4,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[568.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A6TH93",95.4,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[569.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A0H3GLD4",95.4,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[570.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A0H3GLD4",95.4,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[571.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A0H3GLD4",95.4,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[572.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A378AZ23",95.1,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[573.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A378AZ23",95.1,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[574.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A378AZ23",95.1,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[575.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","A0A378AZ23",89.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[576.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","A6TH93",89.4,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[577.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","A0A0H3GLD4",89.4,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[578.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02109","Hadacidin","experimental","unknown"]
[579.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[580.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[581.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[582.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[583.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[584.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[585.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[586.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[587.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02109","Hadacidin","experimental","unknown"]
[588.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[589.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[590.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[591.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[592.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[593.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[594.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[595.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[596.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[597.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[598.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[599.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[600.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[601.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[602.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[603.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[604.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[605.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","A0A377Z7K9",95.1,0.0,"guaA_1 NCTC5050_01199","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000256|SAAS:SAAS01124569};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[606.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","A0A378EBK9",95.8,0.0,"guaA_1 guaA NCTC5046_04830","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS00723675}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS01117722};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[607.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","A0A0H3GRL9",96.0,0.0,"guaA KPHS_39070","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS00723675}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS01117722};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[608.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","A6TCC2",96.0,0.0,"guaA KPN78578_27820 KPN_02833","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-Rule:MF_00344}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00344};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"K.pneumoniae FBA+FVA","index":1,"n_rows":610,"n_cols":19,"rows_kept":610,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","G0LD09",54.5,3.399999999999999E-147,"ugd KPR_11496 NCTC5046_05057",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB01713","Udp-Alpha-D-Xylopyranose","experimental","unknown"]
[1.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","G0LD09",54.5,3.399999999999999E-147,"ugd KPR_11496 NCTC5046_05057",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB03041","UDP-alpha-D-glucuronic acid","experimental","unknown"]
[2.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A0A377ZCW7",54.5,6.899999999999998E-147,"ugd NCTC5050_01747",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB01713","Udp-Alpha-D-Xylopyranose","experimental","unknown"]
[3.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A0A377ZCW7",54.5,6.899999999999998E-147,"ugd NCTC5050_01747",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB03041","UDP-alpha-D-glucuronic acid","experimental","unknown"]
[4.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A6TBE0",54.5,6.899999999999998E-147,"ugd KPN_02493",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB01713","Udp-Alpha-D-Xylopyranose","experimental","unknown"]
[5.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A6TBE0",54.5,6.899999999999998E-147,"ugd KPN_02493",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB03041","UDP-alpha-D-glucuronic acid","experimental","unknown"]
[6.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A0A0H3GV84",54.5,6.899999999999998E-147,"KPHS_35540",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB01713","Udp-Alpha-D-Xylopyranose","experimental","unknown"]
[7.0,"1.1.1.22","UDP-glucose 6-dehydrogenase","Streptococcus pyogenes","P0C0F4","BE0002000","A0A0H3GV84",54.5,6.899999999999998E-147,"KPHS_35540",null,null,"CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};",null,"DB03041","UDP-alpha-D-glucuronic acid","experimental","unknown"]
[8.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A378EC02",90.7,0.0,"hisD_1 NCTC5046_05089","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|RuleBase:RU000580}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|RuleBase:RU000580};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[9.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A378EC02",90.7,0.0,"hisD_1 NCTC5046_05089","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|RuleBase:RU000580}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|RuleBase:RU000580};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[10.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A378EC02",90.7,0.0,"hisD_1 NCTC5046_05089","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|RuleBase:RU000580}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|RuleBase:RU000580};",null,"DB09462","Glycerin","approved, investigational","unknown"]
[11.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A378EC02",90.7,0.0,"hisD_1 NCTC5046_05089","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|RuleBase:RU000580}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|RuleBase:RU000580};",null,"DB03811","Histidinol","experimental","unknown"]
[12.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A377ZBQ0",88.4,0.0,"hisD_2 hisD NCTC5050_01774","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[13.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A377ZBQ0",88.4,0.0,"hisD_2 hisD NCTC5050_01774","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[14.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A377ZBQ0",88.4,0.0,"hisD_2 hisD NCTC5050_01774","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB09462","Glycerin","approved, investigational","unknown"]
[15.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A377ZBQ0",88.4,0.0,"hisD_2 hisD NCTC5050_01774","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03811","Histidinol","experimental","unknown"]
[16.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A6TBC3",88.5,0.0,"hisD KPN_02476","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[17.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A6TBC3",88.5,0.0,"hisD KPN_02476","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[18.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A6TBC3",88.5,0.0,"hisD KPN_02476","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB09462","Glycerin","approved, investigational","unknown"]
[19.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A6TBC3",88.5,0.0,"hisD KPN_02476","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03811","Histidinol","experimental","unknown"]
[20.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A0H3GQM4",88.2,0.0,"hisD KPHS_35370","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[21.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A0H3GQM4",88.2,0.0,"hisD KPHS_35370","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[22.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A0H3GQM4",88.2,0.0,"hisD KPHS_35370","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB09462","Glycerin","approved, investigational","unknown"]
[23.0,"1.1.1.23","Histidinol dehydrogenase","Escherichia coli (strain K12)","P06988","BE0001751","A0A0H3GQM4",88.2,0.0,"hisD KPHS_35370","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. ","FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728939}.","CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};",null,"DB03811","Histidinol","experimental","unknown"]
[24.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A6T4H8",92.3,1.8999999999999994E-177,"dapB KPN78578_00380 KPN_00039","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[25.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A6T4H8",92.3,1.8999999999999994E-177,"dapB KPN78578_00380 KPN_00039","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[26.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A0H3GN28",92.3,1.8999999999999994E-177,"dapB KPHS_07490","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[27.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A0H3GN28",92.3,1.8999999999999994E-177,"dapB KPHS_07490","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[28.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A378C3R8",92.3,1.8999999999999994E-177,"dapB NCTC5050_06692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[29.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A378C3R8",92.3,1.8999999999999994E-177,"dapB NCTC5050_06692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[30.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A378E9V1",91.6,5.199999999999998E-175,"dapB NCTC5046_04201","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[31.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","A0A378E9V1",91.6,5.199999999999998E-175,"dapB NCTC5046_04201","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[32.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A0H3H447",73.4,0.0,"asd KPHS_49510","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[33.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A0H3H447",73.4,0.0,"asd KPHS_49510","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[34.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A0H3H447",73.4,0.0,"asd KPHS_49510","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB04498","Aspartate Semialdehyde","experimental","unknown"]
[35.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378AP86",70.9,1.0999999999999999E-179,"asd_1 asd NCTC5050_02692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[36.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378AP86",70.9,1.0999999999999999E-179,"asd_1 asd NCTC5050_02692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[37.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378AP86",70.9,1.0999999999999999E-179,"asd_1 asd NCTC5050_02692","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB04498","Aspartate Semialdehyde","experimental","unknown"]
[38.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A6TF52",73.4,0.0,"asd KPN_03799","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[39.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A6TF52",73.4,0.0,"asd KPN_03799","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[40.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A6TF52",73.4,0.0,"asd KPN_03799","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB04498","Aspartate Semialdehyde","experimental","unknown"]
[41.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378E6L7",73.4,0.0,"asd NCTC5046_02977","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[42.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378E6L7",73.4,0.0,"asd NCTC5046_02977","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[43.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","A0A378E6L7",73.4,0.0,"asd NCTC5046_02977","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.","CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000256|HAMAP-Rule:MF_02121};",null,"DB04498","Aspartate Semialdehyde","experimental","unknown"]
[44.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A0A378E7A2",78.4,0.0,"murB NCTC5046_02664","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[45.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A0A378E7A2",78.4,0.0,"murB NCTC5046_02664","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[46.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A6TGM9",78.7,0.0,"murB KPN_04350","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[47.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A6TGM9",78.7,0.0,"murB KPN_04350","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[48.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A0A0H3GPZ2",78.7,0.0,"murB KPHS_01910","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[49.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","A0A0H3GPZ2",78.7,0.0,"murB KPHS_01910","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098160}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS01115694};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[50.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A6TD48",93.7,0.0,"cysI KPN78578_30580 KPN_03118","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. {ECO:0000255|HAMAP-Rule:MF_01540}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01540};",null,"DB02832","Siroheme","experimental","unknown"]
[51.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A0A377Z6G5",97.4,0.0,"cysI_1 NCTC5050_00849",{"$nulls":4},"DB02832","Siroheme","experimental","unknown"]
[52.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A0A377Z5D9",89.3,0.0,"cysI_2 NCTC5050_00850","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. {ECO:0000256|SAAS:SAAS00081128}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01116127};",null,"DB02832","Siroheme","experimental","unknown"]
[53.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A0A378DJI4",94.9,0.0,"cysI_2 NCTC5046_01659",{"$nulls":4},"DB02832","Siroheme","experimental","unknown"]
[54.0,"1.8.1.2","Sulfite reductase [NADPH] hemoprotein beta-component","Escherichia coli (strain K12)","P17846","BE0001900","A0A0H3GXH1",93.5,0.0,"cysI KPHS_41930","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. {ECO:0000256|HAMAP-Rule:MF_01540, ECO:0000256|SAAS:SAAS00081128}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01540, ECO:0000256|SAAS:SAAS01116127};",null,"DB02832","Siroheme","experimental","unknown"]
[55.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A6TD49",90.3,0.0,"cysJ KPN78578_30590 KPN_03119","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000255|HAMAP-Rule:MF_01541}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01541};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[56.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A6TD49",90.3,0.0,"cysJ KPN78578_30590 KPN_03119","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000255|HAMAP-Rule:MF_01541}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01541};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[57.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A0H3GWU1",90.3,0.0,"cysJ KPHS_41940","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS01115428};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[58.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A0H3GWU1",90.3,0.0,"cysJ KPHS_41940","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|SAAS:SAAS01115428};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[59.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A377Z696",90.2,0.0,"cysJ NCTC5050_00848",{"$nulls":4},"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[60.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A377Z696",90.2,0.0,"cysJ NCTC5050_00848",{"$nulls":4},"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[61.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A378DJ97",91.1,0.0,"cysJ NCTC5046_01660","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01115428};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[62.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","A0A378DJ97",91.1,0.0,"cysJ NCTC5046_01660","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01115428};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[63.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[64.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[65.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[66.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[67.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[68.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[69.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[70.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[71.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[72.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[73.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[74.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[75.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[76.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[77.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[78.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[79.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[80.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[81.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[82.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[83.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[84.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A6TDG3",94.3,0.0,"thyA KPN78578_31730 KPN_03236","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[85.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[86.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[87.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[88.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03038","LY341770","experimental","unknown"]
[89.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[90.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[91.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[92.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[93.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03558","Sp-876","experimental","unknown"]
[94.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[95.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[96.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[97.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[98.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[99.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[100.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[101.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04503","Sp-722","experimental","unknown"]
[102.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[103.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04586","2-bromophenol","experimental","unknown"]
[104.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[105.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[106.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A378EEU5",93.9,0.0,"thyA NCTC5046_05316","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[107.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[108.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[109.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[110.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03038","LY341770","experimental","unknown"]
[111.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[112.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[113.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[114.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[115.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03558","Sp-876","experimental","unknown"]
[116.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[117.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[118.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[119.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[120.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[121.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[122.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[123.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04503","Sp-722","experimental","unknown"]
[124.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[125.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04586","2-bromophenol","experimental","unknown"]
[126.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[127.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[128.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","A0A0H3GX29",93.9,0.0,"thyA KPHS_42990","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[129.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Shigella flexneri","P0A789","BE0001928","A0A0H3GMI1",93.9,0.0,"pyrB KPHS_05040","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00001};",null,"DB03459","Sparfosic acid","experimental","unknown"]
[130.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Shigella flexneri","P0A789","BE0001928","A0A378B0J6",93.9,0.0,"pyrB NCTC5050_03825","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00001};",null,"DB03459","Sparfosic acid","experimental","unknown"]
[131.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Shigella flexneri","P0A789","BE0001928","A6THH4",93.9,0.0,"pyrB KPN78578_45840 KPN_04657","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00001};",null,"DB03459","Sparfosic acid","experimental","unknown"]
[132.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Escherichia coli (strain K12)","P0A786","BE0003341","A0A0H3GMI1",93.9,0.0,"pyrB KPHS_05040","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00001};",null,"DB05540","Alanosine","investigational","unknown"]
[133.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Escherichia coli (strain K12)","P0A786","BE0003341","A0A378B0J6",93.9,0.0,"pyrB NCTC5050_03825","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00001};",null,"DB05540","Alanosine","investigational","unknown"]
[134.0,"2.1.3.2","Aspartate carbamoyltransferase catalytic chain","Escherichia coli (strain K12)","P0A786","BE0003341","A6THH4",93.9,0.0,"pyrB KPN78578_45840 KPN_04657","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00001};",null,"DB05540","Alanosine","investigational","unknown"]
[135.0,"2.1.3.3","Ornithine carbamoyltransferase chain I","Escherichia coli (strain K12)","P04391","BE0001875","A0A0H3GHJ1",88.9,0.0,"KPHS_05120",null,"FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. {ECO:0000256|SAAS:SAAS00009102}.","CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|SAAS:SAAS01125822};",null,"DB02965","Ndelta-(N'-Sulphodiaminophosphinyl)-L-Ornithine","experimental","unknown"]
[136.0,"2.1.3.3","Ornithine carbamoyltransferase chain I","Escherichia coli (strain K12)","P04391","BE0001875","A6THH6",89.2,0.0,"argI KPN_04659","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3. ","FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. {ECO:0000256|SAAS:SAAS00009102}.","CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|SAAS:SAAS01125822};",null,"DB02965","Ndelta-(N'-Sulphodiaminophosphinyl)-L-Ornithine","experimental","unknown"]
[137.0,"2.1.3.3","Ornithine carbamoyltransferase chain I","Escherichia coli (strain K12)","P04391","BE0001875","A0A378B121",89.2,0.0,"argI NCTC5050_03827",null,"FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. {ECO:0000256|SAAS:SAAS00009102}.","CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|SAAS:SAAS01125822};",null,"DB02965","Ndelta-(N'-Sulphodiaminophosphinyl)-L-Ornithine","experimental","unknown"]
[138.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[139.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03134","2-Aminopimelic Acid","experimental","unknown"]
[140.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01856","Pimelic Acid","experimental","unknown"]
[141.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03699","Succinyl-Coenzyme A","experimental","unknown"]
[142.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378C0N6",96.4,0.0,"dapD NCTC10313_01570 NCTC5050_06498","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03905","Succinamide-Coa","experimental","unknown"]
[143.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[144.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03134","2-Aminopimelic Acid","experimental","unknown"]
[145.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01856","Pimelic Acid","experimental","unknown"]
[146.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03699","Succinyl-Coenzyme A","experimental","unknown"]
[147.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A0H3GMV1",96.4,0.0,"dapD KPHS_09130","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03905","Succinamide-Coa","experimental","unknown"]
[148.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[149.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03134","2-Aminopimelic Acid","experimental","unknown"]
[150.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB01856","Pimelic Acid","experimental","unknown"]
[151.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03699","Succinyl-Coenzyme A","experimental","unknown"]
[152.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A0A378EA89",96.4,0.0,"dapD NCTC5046_04389","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS01124328};",null,"DB03905","Succinamide-Coa","experimental","unknown"]
[153.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[154.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB03134","2-Aminopimelic Acid","experimental","unknown"]
[155.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB01856","Pimelic Acid","experimental","unknown"]
[156.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB03699","Succinyl-Coenzyme A","experimental","unknown"]
[157.0,"2.3.1.117","2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase","Unknown prokaryotic organism","P56220","BE0001297","A6T4W8",96.4,0.0,"dapD KPN78578_01780 KPN_00179","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. ",null,"CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000255|HAMAP-Rule:MF_00811};",null,"DB03905","Succinamide-Coa","experimental","unknown"]
[158.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A0H3GMW8",42.4,5.4000000000000005E-58,"lpxA KPHS_09280","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[159.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A0H3GMW8",42.4,5.4000000000000005E-58,"lpxA KPHS_09280","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[160.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A6T4Y3",42.4,5.4000000000000005E-58,"lpxA KPN78578_01930 KPN_00194","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-Rule:MF_00387};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[161.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A6T4Y3",42.4,5.4000000000000005E-58,"lpxA KPN78578_01930 KPN_00194","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-Rule:MF_00387};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[162.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A378C0J0",42.4,2.7000000000000002E-58,"lpxA NCTC10313_01586 NCTC5050_06478","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[163.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A378C0J0",42.4,2.7000000000000002E-58,"lpxA NCTC10313_01586 NCTC5050_06478","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[164.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A378EC06",42.4,2.7000000000000002E-58,"lpxA NCTC5046_04408","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[165.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","A0A378EC06",42.4,2.7000000000000002E-58,"lpxA NCTC5046_04408","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[166.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB09414","Dipotassium phosphate","approved","unknown"]
[167.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08407","PLATENSIMYCIN","experimental","unknown"]
[168.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB03017","Lauric Acid","approved, experimental","unknown"]
[169.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB01034","Cerulenin","approved","yes","inhibitor"]
[170.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A0H3GLG4",95.3,0.0,"KPHS_19720","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08366","3-({3-[(1S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxodecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid","experimental","unknown"]
[171.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB09414","Dipotassium phosphate","approved","unknown"]
[172.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08407","PLATENSIMYCIN","experimental","unknown"]
[173.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB03017","Lauric Acid","approved, experimental","unknown"]
[174.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB01034","Cerulenin","approved","yes","inhibitor"]
[175.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A6T7F5",95.4,0.0,"fabF KPN_01093","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08366","3-({3-[(1S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxodecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid","experimental","unknown"]
[176.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB09414","Dipotassium phosphate","approved","unknown"]
[177.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08407","PLATENSIMYCIN","experimental","unknown"]
[178.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB03017","Lauric Acid","approved, experimental","unknown"]
[179.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB01034","Cerulenin","approved","yes","inhibitor"]
[180.0,"2.3.1.179","3-oxoacyl-[acyl-carrier-protein] synthase 2","Escherichia coli (strain K12)","P0AAI5","BE0000800","A0A377ZBZ2",95.4,0.0,"fabF_1 NCTC5050_01823","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.","CATALYTIC ACTIVITY: Reaction=(11Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(13Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:14565, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9921, Rhea:RHEA-COMP:9922, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78778, ChEBI:CHEBI:78779; EC=2.3.1.179; Evidence={ECO:0000256|PIRNR:PIRNR000447};",null,"DB08366","3-({3-[(1S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxodecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid","experimental","unknown"]
[181.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[182.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[183.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[184.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[185.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[186.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[187.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[188.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A377ZAM0",96.5,1.1999999999999995E-179,"fabB_2 NCTC5050_01417",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[189.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[190.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[191.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[192.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[193.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[194.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[195.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[196.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A6TC09",96.5,0.0,"fabB KPN_02713",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[197.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[198.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[199.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[200.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[201.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[202.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[203.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[204.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A378CQJ7",96.3,0.0,"fabB NCTC5046_00576",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[205.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[206.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[207.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[208.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[209.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[210.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[211.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[212.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","A0A0H3GR90",96.5,0.0,"KPHS_37820",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[213.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","A6T4N3",89.6,0.0,"murG KPN78578_00930 KPN_00094","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[214.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","A0A0H3GJ97",89.6,0.0,"murG KPHS_08100","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00765558}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS01124123};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[215.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","A0A378EBK5",88.7,1.7999999999999995E-147,"murG_2 NCTC5046_04271","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000256|SAAS:SAAS00765558}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000256|SAAS:SAAS01124123};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[216.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","A0A378C1B0",88.1,1.5999999999999996E-144,"murG_1 NCTC5050_06619","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000256|SAAS:SAAS00765558}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000256|SAAS:SAAS01124123};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[217.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A0H3GXD7",93.4,1.1999999999999995E-139,"pyrE KPHS_51450","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[218.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A0H3GXD7",93.4,1.1999999999999995E-139,"pyrE KPHS_51450","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[219.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A6TFN4",93.9,1.3999999999999994E-140,"pyrE KPN78578_39440 KPN_03983","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[220.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A6TFN4",93.9,1.3999999999999994E-140,"pyrE KPN78578_39440 KPN_03983","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[221.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A378AUX2",90.1,2.2999999999999992E-77,"pyrE NCTC5050_03219","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[222.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A378AUX2",90.1,2.2999999999999992E-77,"pyrE NCTC5050_03219","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[223.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A378E7H8",93.9,8.1999999999999975E-140,"pyrE NCTC5046_02750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[224.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","A0A378E7H8",93.9,8.1999999999999975E-140,"pyrE NCTC5046_02750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[225.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A6TBZ8",96.6,0.0,"purF KPN_02702","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[226.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A6TBZ8",96.6,0.0,"purF KPN_02702","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[227.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A6TBZ8",96.6,0.0,"purF KPN_02702","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[228.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A378CQK2",96.6,0.0,"purF NCTC5046_00589","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[229.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A378CQK2",96.6,0.0,"purF NCTC5046_00589","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[230.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A378CQK2",96.6,0.0,"purF NCTC5046_00589","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[231.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A377Z9V1",96.6,0.0,"purF NCTC10313_04977 NCTC5050_01433","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[232.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A377Z9V1",96.6,0.0,"purF NCTC10313_04977 NCTC5050_01433","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[233.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A377Z9V1",96.6,0.0,"purF NCTC10313_04977 NCTC5050_01433","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[234.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A0H3H133",96.6,0.0,"purF KPHS_37710","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[235.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A0H3H133",96.6,0.0,"purF KPHS_37710","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[236.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","A0A0H3H133",96.6,0.0,"purF KPHS_37710","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[237.0,"2.4.2.17","ATP phosphoribosyltransferase","Escherichia coli (strain K12)","P60757","BE0001228","A0A377ZDD3",94.0,0.0,"hisG NCTC10313_04649 NCTC5050_01775","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. ","FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. {ECO:0000256|HAMAP-Rule:MF_00079}.","CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17; Evidence={ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS01121154};",null,"DB01661","Phosphoribosyl Atp","experimental","unknown"]
[238.0,"2.4.2.17","ATP phosphoribosyltransferase","Escherichia coli (strain K12)","P60757","BE0001228","A6TBC2",94.0,0.0,"hisG KPN78578_24320 KPN_02475","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. ","FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. {ECO:0000255|HAMAP-Rule:MF_00079}.","CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00079};",null,"DB01661","Phosphoribosyl Atp","experimental","unknown"]
[239.0,"2.4.2.17","ATP phosphoribosyltransferase","Escherichia coli (strain K12)","P60757","BE0001228","A0A378EE61",93.8,4.6999999999999986E-114,"hisG_2 NCTC5046_05092","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. ","FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. {ECO:0000256|SAAS:SAAS00046314}.","CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17; Evidence={ECO:0000256|SAAS:SAAS01121154};",null,"DB01661","Phosphoribosyl Atp","experimental","unknown"]
[240.0,"2.4.2.17","ATP phosphoribosyltransferase","Escherichia coli (strain K12)","P60757","BE0001228","A0A0H3H0I5",94.0,0.0,"hisG KPHS_35360","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. ","FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. {ECO:0000256|HAMAP-Rule:MF_00079}.","CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17; Evidence={ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS01121154};",null,"DB01661","Phosphoribosyl Atp","experimental","unknown"]
[241.0,"2.4.2.18","Anthranilate phosphoribosyltransferase","Erwinia carotovora","Q8VP84","BE0002489","A6T7W8",73.1,6.399999999999999E-169,"trpD KPN_01256","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. ","FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS00918330}.","CATALYTIC ACTIVITY: Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18; Evidence={ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01124167};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[242.0,"2.4.2.18","Anthranilate phosphoribosyltransferase","Erwinia carotovora","Q8VP84","BE0002489","A0A0H3GLX6",73.1,6.399999999999999E-169,"trpD KPHS_21620","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. ","FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS00918330}.","CATALYTIC ACTIVITY: Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18; Evidence={ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01124167};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[243.0,"2.4.2.18","Anthranilate phosphoribosyltransferase","Erwinia carotovora","Q8VP84","BE0002489","A0A378EHA3",72.8,2.5999999999999996E-168,"trpD NCTC5046_07037","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. ","FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS00918330}.","CATALYTIC ACTIVITY: Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18; Evidence={ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01124167};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[244.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378BNF7",88.7,5.4E-174,"aroA_2 NCTC5050_05393","Metabolic intermediate biosynthesis; chorismate biosynthesis. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|SAAS:SAAS01118199};",null,"DB03116","5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate","experimental","unknown"]
[245.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378BNF7",88.7,5.4E-174,"aroA_2 NCTC5050_05393","Metabolic intermediate biosynthesis; chorismate biosynthesis. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|SAAS:SAAS01118199};",null,"DB01942","Formic Acid","approved, experimental","unknown"]
[246.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378BNF7",88.7,5.4E-174,"aroA_2 NCTC5050_05393","Metabolic intermediate biosynthesis; chorismate biosynthesis. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown"]
[247.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378BNF7",88.7,5.4E-174,"aroA_2 NCTC5050_05393","Metabolic intermediate biosynthesis; chorismate biosynthesis. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[248.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A6T701",89.0,0.0,"aroA KPN78578_09110 KPN_00936","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00210};",null,"DB03116","5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate","experimental","unknown"]
[249.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A6T701",89.0,0.0,"aroA KPN78578_09110 KPN_00936","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00210};",null,"DB01942","Formic Acid","approved, experimental","unknown"]
[250.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A6T701",89.0,0.0,"aroA KPN78578_09110 KPN_00936","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00210};",null,"DB04539","Glyphosate","experimental","unknown"]
[251.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A6T701",89.0,0.0,"aroA KPN78578_09110 KPN_00936","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00210};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[252.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378DHG0",89.0,0.0,"aroA NCTC5046_01000","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB03116","5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate","experimental","unknown"]
[253.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378DHG0",89.0,0.0,"aroA NCTC5046_01000","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB01942","Formic Acid","approved, experimental","unknown"]
[254.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378DHG0",89.0,0.0,"aroA NCTC5046_01000","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown"]
[255.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A378DHG0",89.0,0.0,"aroA NCTC5046_01000","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[256.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A0H3GV01",89.2,0.0,"aroA KPHS_18160","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB03116","5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate","experimental","unknown"]
[257.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A0H3GV01",89.2,0.0,"aroA KPHS_18160","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB01942","Formic Acid","approved, experimental","unknown"]
[258.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A0H3GV01",89.2,0.0,"aroA KPHS_18160","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown"]
[259.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A6D3","BE0001381","A0A0H3GV01",89.2,0.0,"aroA KPHS_18160","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00378958}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[260.0,"2.5.1.48","Cystathionine gamma-synthase","Escherichia coli (strain K12)","P00935","BE0003209","A0A378E8P3",95.8,0.0,"metB NCTC5046_03255",{"$nulls":4},"DB04083","N'-Pyridoxyl-Lysine-5'-Monophosphate","experimental","unknown"]
[261.0,"2.5.1.48","Cystathionine gamma-synthase","Escherichia coli (strain K12)","P00935","BE0003209","A0A0H3GPP8",95.8,0.0,"KPHS_00860",{"$nulls":4},"DB04083","N'-Pyridoxyl-Lysine-5'-Monophosphate","experimental","unknown"]
[262.0,"2.5.1.48","Cystathionine gamma-synthase","Escherichia coli (strain K12)","P00935","BE0003209","A0A378AUN9",95.8,0.0,"metB NCTC10313_07038 NCTC5050_03330",{"$nulls":4},"DB04083","N'-Pyridoxyl-Lysine-5'-Monophosphate","experimental","unknown"]
[263.0,"2.5.1.48","Cystathionine gamma-synthase","Escherichia coli (strain K12)","P00935","BE0003209","A6TGC8",95.8,0.0,"metB KPN_04233",{"$nulls":4},"DB04083","N'-Pyridoxyl-Lysine-5'-Monophosphate","experimental","unknown"]
[264.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A0H3GUB6",95.4,0.0,"kdsA KPHS_32290","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB01819","Phosphoenolpyruvate","experimental","unknown"]
[265.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A0H3GUB6",95.4,0.0,"kdsA KPHS_32290","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[266.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A0H3GUB6",95.4,0.0,"kdsA KPHS_32290","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[267.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A0H3GUB6",95.4,0.0,"kdsA KPHS_32290","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[268.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378EE77",95.4,0.0,"kdsA NCTC5046_05810","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB01819","Phosphoenolpyruvate","experimental","unknown"]
[269.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378EE77",95.4,0.0,"kdsA NCTC5046_05810","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[270.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378EE77",95.4,0.0,"kdsA NCTC5046_05810","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[271.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378EE77",95.4,0.0,"kdsA NCTC5046_05810","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[272.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378BC15",95.4,0.0,"kdsA NCTC5050_04802","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB01819","Phosphoenolpyruvate","experimental","unknown"]
[273.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378BC15",95.4,0.0,"kdsA NCTC5050_04802","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[274.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378BC15",95.4,0.0,"kdsA NCTC5050_04802","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[275.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A0A378BC15",95.4,0.0,"kdsA NCTC5050_04802","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS01123735};",null,"DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[276.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A6TAN5",95.4,0.0,"kdsA KPN78578_21950 KPN_02230","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000255|HAMAP-Rule:MF_00056};",null,"DB01819","Phosphoenolpyruvate","experimental","unknown"]
[277.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A6TAN5",95.4,0.0,"kdsA KPN78578_21950 KPN_02230","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000255|HAMAP-Rule:MF_00056};",null,"DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[278.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A6TAN5",95.4,0.0,"kdsA KPN78578_21950 KPN_02230","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000255|HAMAP-Rule:MF_00056};",null,"DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[279.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","A6TAN5",95.4,0.0,"kdsA KPN78578_21950 KPN_02230","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; Evidence={ECO:0000255|HAMAP-Rule:MF_00056};",null,"DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[280.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[281.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[282.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[283.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[284.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378E6U7",93.9,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[285.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[286.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[287.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[288.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[289.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A6TEK8",93.6,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[290.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[291.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[292.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[293.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[294.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A0H3GYZ6",93.6,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[295.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[296.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[297.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[298.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[299.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","A0A378AHV3",93.6,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[300.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","A6TEK8",92.1,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[301.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","A0A378E6U7",92.4,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[302.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","A0A0H3GYZ6",92.1,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[303.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","A0A378AHV3",92.1,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[304.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","A0A378E6U7",92.4,0.0,"murA_2 NCTC5046_02521","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|SAAS:SAAS01124343};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[305.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","A0A0H3GYZ6",92.1,0.0,"murA KPHS_47380","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[306.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","A0A378AHV3",92.1,0.0,"murA NCTC5050_02435","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[307.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","A6TEK8",92.1,0.0,"murA KPN78578_35680 KPN_03599","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[308.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[309.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[310.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[311.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[312.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[313.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378E908",92.0,0.0,"glmS_1 glmS NCTC5046_03130",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[314.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[315.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[316.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[317.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[318.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[319.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A0H3H4X5",92.0,0.0,"glmS KPHS_53010",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[320.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[321.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[322.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[323.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[324.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[325.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A0A378ARM3",92.3,0.0,"glmS_1 glmS NCTC5050_03000",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[326.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[327.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[328.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[329.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[330.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[331.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","A6TG33",92.4,0.0,"glmS KPN_04134",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[332.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A0H3GPS2",94.8,0.0,"ilvE KPHS_01160","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[333.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A0H3GPS2",94.8,0.0,"ilvE KPHS_01160","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03553","Glutaric Acid","experimental","unknown"]
[334.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A0H3GPS2",94.8,0.0,"ilvE KPHS_01160","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03993","4-Methyl Valeric Acid","experimental","unknown"]
[335.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A0H3GPS2",94.8,0.0,"ilvE KPHS_01160","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB04063","2-Methylleucine","experimental","unknown"]
[336.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A6TGF7",94.8,0.0,"ilvE KPN_04269","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[337.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A6TGF7",94.8,0.0,"ilvE KPN_04269","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03553","Glutaric Acid","experimental","unknown"]
[338.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A6TGF7",94.8,0.0,"ilvE KPN_04269","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03993","4-Methyl Valeric Acid","experimental","unknown"]
[339.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A6TGF7",94.8,0.0,"ilvE KPN_04269","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB04063","2-Methylleucine","experimental","unknown"]
[340.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378AS62",94.8,0.0,"ilvE NCTC5050_02940","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[341.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378AS62",94.8,0.0,"ilvE NCTC5050_02940","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03553","Glutaric Acid","experimental","unknown"]
[342.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378AS62",94.8,0.0,"ilvE NCTC5050_02940","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03993","4-Methyl Valeric Acid","experimental","unknown"]
[343.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378AS62",94.8,0.0,"ilvE NCTC5050_02940","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB04063","2-Methylleucine","experimental","unknown"]
[344.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378E787",94.7,2.8999999999999992E-114,"ilvE_1 ilvE NCTC5046_03301","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[345.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378E787",94.7,2.8999999999999992E-114,"ilvE_1 ilvE NCTC5046_03301","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03553","Glutaric Acid","experimental","unknown"]
[346.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378E787",94.7,2.8999999999999992E-114,"ilvE_1 ilvE NCTC5046_03301","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB03993","4-Methyl Valeric Acid","experimental","unknown"]
[347.0,"2.6.1.42","Branched-chain-amino-acid aminotransferase","Escherichia coli (strain K12)","P0AB80","BE0002016","A0A378E787",94.7,2.8999999999999992E-114,"ilvE_1 ilvE NCTC5046_03301","Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. ","FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU364094};",null,"DB04063","2-Methylleucine","experimental","unknown"]
[348.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A377ZEZ0",85.3,6.499999999999999E-137,"hisC_2 NCTC5050_01772",{"$nulls":4},"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[349.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A377ZEZ0",85.3,6.499999999999999E-137,"hisC_2 NCTC5050_01772",{"$nulls":4},"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[350.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A377ZEZ0",85.3,6.499999999999999E-137,"hisC_2 NCTC5050_01772",{"$nulls":4},"DB03997","L-histidinol phosphate","experimental","unknown"]
[351.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A0H3GVS5",84.1,0.0,"hisC KPHS_35380","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[352.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A0H3GVS5",84.1,0.0,"hisC KPHS_35380","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[353.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A0H3GVS5",84.1,0.0,"hisC KPHS_35380","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB03997","L-histidinol phosphate","experimental","unknown"]
[354.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A378EDY0",84.1,0.0,"hisC NCTC5046_05088","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[355.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A378EDY0",84.1,0.0,"hisC NCTC5046_05088","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[356.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A0A378EDY0",84.1,0.0,"hisC NCTC5046_05088","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};",null,"DB03997","L-histidinol phosphate","experimental","unknown"]
[357.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A6TBC4",84.4,0.0,"hisC KPN78578_24340 KPN_02477","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB01813","Pyridoxyl-Glutamic Acid-5'-Monophosphate","experimental","unknown"]
[358.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A6TBC4",84.4,0.0,"hisC KPN78578_24340 KPN_02477","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[359.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Escherichia coli (strain K12)","P06986","BE0001396","A6TBC4",84.4,0.0,"hisC KPN78578_24340 KPN_02477","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB03997","L-histidinol phosphate","experimental","unknown"]
[360.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E8W0",93.8,5.9E-43,"argB_2 NCTC5046_03277",{"$nulls":4},"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[361.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E8W0",93.8,5.9E-43,"argB_2 NCTC5046_03277",{"$nulls":4},"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[362.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E8W0",93.8,5.9E-43,"argB_2 NCTC5046_03277",{"$nulls":4},"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[363.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E7A4",91.9,3.9999999999999993E-106,"argB_1 NCTC5046_03276","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|SAAS:SAAS01124576};",null,"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[364.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E7A4",91.9,3.9999999999999993E-106,"argB_1 NCTC5046_03276","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|SAAS:SAAS01124576};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[365.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378E7A4",91.9,3.9999999999999993E-106,"argB_1 NCTC5046_03276","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|SAAS:SAAS01124576};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[366.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A6TGE3",93.0,3.2999999999999996E-166,"argB KPN78578_42030 KPN_04248","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00082};",null,"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[367.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A6TGE3",93.0,3.2999999999999996E-166,"argB KPN78578_42030 KPN_04248","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00082};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[368.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A6TGE3",93.0,3.2999999999999996E-166,"argB KPN78578_42030 KPN_04248","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00082};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[369.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A0H3GPQ8",93.0,1.2999999999999998E-165,"argB KPHS_01010","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[370.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A0H3GPQ8",93.0,1.2999999999999998E-165,"argB KPHS_01010","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[371.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A0H3GPQ8",93.0,1.2999999999999998E-165,"argB KPHS_01010","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[372.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378AUU7",92.6,2.9999999999999985E-164,"argB NCTC5050_03349","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04444","Tetrafluoroaluminate Ion","experimental","unknown"]
[373.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378AUU7",92.6,2.9999999999999985E-164,"argB NCTC5050_03349","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[374.0,"2.7.2.8","Acetylglutamate kinase","Escherichia coli (strain K12)","P0A6C8","BE0001589","A0A378AUU7",92.6,2.9999999999999985E-164,"argB NCTC5050_03349","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01076979}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[375.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","A6T7F8",84.3,1.4999999999999995E-119,"tmk KPN78578_10680 KPN_01096",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000255|HAMAP-Rule:MF_00165}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00165};",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[376.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","A0A0H3GMT6",84.3,1.4999999999999995E-119,"tmk KPHS_19750",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-Rule:MF_00165}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[377.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","A0A377ZWF0",84.3,1.4999999999999995E-119,"tmk NCTC10313_04311 NCTC5050_01826",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-Rule:MF_00165}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[378.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","A0A378CRW1",83.8,4.399999999999999E-119,"tmk NCTC5046_00789",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-Rule:MF_00165}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[379.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","A0A378E8H7",68.6,0.0,"glmU NCTC5046_03131","Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083685}.","CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124206}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124218};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[380.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","A0A0H3GVB1",68.9,0.0,"glmU KPHS_53020","Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083685}.","CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124206}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124218};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[381.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","A6TG34",68.6,0.0,"glmU KPN78578_40940 KPN_04135","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[382.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","A0A0H3GTS8",41.7,1.9E-33,"KPHS_47470","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. ","FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[383.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","A0A378AHM5",41.1,5.4E-33,"kdsC NCTC10313_00960 NCTC5050_02446","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. ","FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[384.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","A6TEL7",41.7,1.9E-33,"yrbI KPN_03608","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. ","FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[385.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","A0A378E6Z2",41.7,1.9E-33,"kdsC NCTC5046_02530","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. ","FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[386.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A378CRM0",89.1,0.0,"pyrC_2 pyrC NCTC5046_00750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[387.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A378CRM0",89.1,0.0,"pyrC_2 pyrC NCTC5046_00750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[388.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A378CRM0",89.1,0.0,"pyrC_2 pyrC NCTC5046_00750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[389.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A378CRM0",89.1,0.0,"pyrC_2 pyrC NCTC5046_00750","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[390.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A377ZDG2",89.4,0.0,"pyrC NCTC5050_01794","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[391.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A377ZDG2",89.4,0.0,"pyrC NCTC5050_01794","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[392.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A377ZDG2",89.4,0.0,"pyrC NCTC5050_01794","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[393.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A0A377ZDG2",89.4,0.0,"pyrC NCTC5050_01794","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|SAAS:SAAS01090757}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00219, ECO:0000256|RuleBase:RU003440, ECO:0000256|SAAS:SAAS01124551};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[394.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A6T7D6",89.7,0.0,"pyrC KPN78578_10460 KPN_01074","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[395.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A6T7D6",89.7,0.0,"pyrC KPN78578_10460 KPN_01074","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[396.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A6T7D6",89.7,0.0,"pyrC KPN78578_10460 KPN_01074","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[397.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","A6T7D6",89.7,0.0,"pyrC KPN78578_10460 KPN_01074","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[398.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A378EEI5",87.1,0.0,"lysA NCTC5046_05290","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[399.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A378EEI5",87.1,0.0,"lysA NCTC5046_05290","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03252","D-Lysine","experimental","unknown"]
[400.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A377Z4Z0",87.1,0.0,"lysA lysA_1 NCTC10313_05801 NCTC5050_00670","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[401.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A377Z4Z0",87.1,0.0,"lysA lysA_1 NCTC10313_05801 NCTC5050_00670","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03252","D-Lysine","experimental","unknown"]
[402.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A0H3GSP6",87.1,0.0,"lysA KPHS_43170","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[403.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A0A0H3GSP6",87.1,0.0,"lysA KPHS_43170","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03252","D-Lysine","experimental","unknown"]
[404.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A6TDH9",87.1,0.0,"lysA KPN_03252","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[405.0,"4.1.1.20","Diaminopimelate decarboxylase","Escherichia coli (strain K12)","P00861","BE0001844","A6TDH9",87.1,0.0,"lysA KPN_03252","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. ","FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-Rule:MF_02120}.","CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};",null,"DB03252","D-Lysine","experimental","unknown"]
[406.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A0A377ZGT0",85.3,2.5999999999999992E-145,"pyrF NCTC10313_04086 NCTC5050_02067","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[407.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A0A377ZGT0",85.3,2.5999999999999992E-145,"pyrF NCTC10313_04086 NCTC5050_02067","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[408.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A6T7Y9",85.5,1.3999999999999997E-136,"pyrF KPN_01277","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[409.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A6T7Y9",85.5,1.3999999999999997E-136,"pyrF KPN_01277","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[410.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A0A0H3GNE4",85.5,1.3999999999999997E-136,"pyrF KPHS_21850","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[411.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","A0A0H3GNE4",85.5,1.3999999999999997E-136,"pyrF KPHS_21850","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[412.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","A0A378EBZ2",56.1,6.599999999999999E-88,"aroD NCTC5046_04243","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[413.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","A0A0H3GMI6",55.7,1.8999999999999998E-87,"aroD KPHS_07880","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[414.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","A0A378C2N8",55.7,1.8999999999999998E-87,"aroD NCTC5050_06648","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[415.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","A6T4L2",56.1,6.599999999999999E-88,"aroD KPN78578_00720 KPN_00073","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[416.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","A0A378C2N8",31.0,2.6E-25,"aroD NCTC5050_06648","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[417.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","A0A378EBZ2",31.0,2.6E-25,"aroD NCTC5046_04243","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[418.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","A0A0H3GMI6",31.0,2.6E-25,"aroD KPHS_07880","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000256|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[419.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","A6T4L2",31.0,2.6E-25,"aroD KPN78578_00720 KPN_00073","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[420.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","A0A378BP67",97.7,9.999999999999999E-123,"fabA NCTC10313_04481 NCTC5050_05321","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[421.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","A0A0H3GL47",97.7,9.999999999999999E-123,"fabA KPHS_18620","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[422.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","A6T748",97.7,9.999999999999999E-123,"fabA KPN78578_09580 KPN_00983","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000255|HAMAP-Rule:MF_00405}.","CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000255|HAMAP-Rule:MF_00405}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000255|HAMAP-Rule:MF_00405}; CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00405};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[423.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","A0A378EC77",97.7,9.999999999999999E-123,"fabA NCTC5046_05152","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[424.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","A6T748",97.7,9.999999999999999E-123,"fabA KPN78578_09580 KPN_00983","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000255|HAMAP-Rule:MF_00405}.","CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000255|HAMAP-Rule:MF_00405}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000255|HAMAP-Rule:MF_00405}; CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00405};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[425.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","A0A378EC77",97.7,9.999999999999999E-123,"fabA NCTC5046_05152","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[426.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","A0A0H3GL47",97.7,9.999999999999999E-123,"fabA KPHS_18620","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[427.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","A0A378BP67",97.7,9.999999999999999E-123,"fabA NCTC10313_04481 NCTC5050_05321","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS00064153}.","CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122664}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122666}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000256|SAAS:SAAS01122660};",null,"DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[428.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","A0A378CQP1",46.4,6.599999999999999E-98,"aroC NCTC5046_00568","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000256|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[429.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","A0A0H3GWE8",46.4,4.599999999999999E-98,"aroC KPHS_37880","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000256|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[430.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","A6TC15",46.4,4.599999999999999E-98,"aroC KPN78578_26750 KPN_02719","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[431.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB03435","Uridine-5'-Diphosphate","experimental","unknown"]
[432.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[433.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB02790","Phenyl-Uridine-5'-Diphosphate","experimental","unknown"]
[434.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB02421","Uridine-5'-Diphosphate-Mannose","experimental","unknown"]
[435.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB04097","Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose","experimental","unknown"]
[436.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A6T6I8",92.9,0.0,"galE KPN_00773",{"$nulls":4},"DB01861","Uridine diphosphate glucose","experimental","unknown"]
[437.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB03435","Uridine-5'-Diphosphate","experimental","unknown"]
[438.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[439.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB02790","Phenyl-Uridine-5'-Diphosphate","experimental","unknown"]
[440.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB02421","Uridine-5'-Diphosphate-Mannose","experimental","unknown"]
[441.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB04097","Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose","experimental","unknown"]
[442.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378BS14",92.6,0.0,"galE NCTC5050_05657",{"$nulls":4},"DB01861","Uridine diphosphate glucose","experimental","unknown"]
[443.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB03435","Uridine-5'-Diphosphate","experimental","unknown"]
[444.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[445.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB02790","Phenyl-Uridine-5'-Diphosphate","experimental","unknown"]
[446.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB02421","Uridine-5'-Diphosphate-Mannose","experimental","unknown"]
[447.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB04097","Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose","experimental","unknown"]
[448.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A378DI54",91.7,4.499999999999998E-143,"galE_1 NCTC5046_01245",{"$nulls":4},"DB01861","Uridine diphosphate glucose","experimental","unknown"]
[449.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB03435","Uridine-5'-Diphosphate","experimental","unknown"]
[450.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[451.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB02790","Phenyl-Uridine-5'-Diphosphate","experimental","unknown"]
[452.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB02421","Uridine-5'-Diphosphate-Mannose","experimental","unknown"]
[453.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB04097","Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose","experimental","unknown"]
[454.0,"5.1.3.2","UDP-glucose 4-epimerase","Escherichia coli (strain K12)","P09147","BE0001901","A0A0H3GLM5",92.9,0.0,"KPHS_15950",{"$nulls":4},"DB01861","Uridine diphosphate glucose","experimental","unknown"]
[455.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A6TFL4",97.4,0.0,"hldD KPN78578_39240 KPN_03963","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[456.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A6TFL4",97.4,0.0,"hldD KPN78578_39240 KPN_03963","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[457.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A0H3GUR3",97.4,0.0,"hldD KPHS_51220","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[458.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A0H3GUR3",97.4,0.0,"hldD KPHS_51220","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[459.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A377YYC3",97.4,0.0,"hldD NCTC10313_00421 NCTC5050_03246","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[460.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A377YYC3",97.4,0.0,"hldD NCTC10313_00421 NCTC5050_03246","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[461.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A378E7F1",97.4,0.0,"hldD NCTC5046_02773","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[462.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","A0A378E7F1",97.4,0.0,"hldD NCTC5046_02773","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS00751121}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01601, ECO:0000256|SAAS:SAAS01121954};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[463.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","A6TEG8",54.9,1.8999999999999996E-70,"diaA KPN78578_35280 KPN_03557",null,"FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. {ECO:0000255|HAMAP-Rule:MF_01157}.",null,null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[464.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","A0A377YYQ4",54.9,1.8999999999999996E-70,"yraO diaA NCTC10313_01032 NCTC5050_02380",null,"FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. {ECO:0000256|HAMAP-Rule:MF_01157, ECO:0000256|SAAS:SAAS00846119}.",null,null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[465.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","A0A0H3GXZ7",54.9,1.8999999999999996E-70,"diaA KPHS_46940",null,"FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. {ECO:0000256|HAMAP-Rule:MF_01157, ECO:0000256|SAAS:SAAS00846119}.",null,null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[466.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","A0A378E6M5",54.9,1.8999999999999996E-70,"yraO diaA NCTC5046_02468",null,"FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. {ECO:0000256|HAMAP-Rule:MF_01157, ECO:0000256|SAAS:SAAS00846119}.",null,null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[467.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A0A377ZAQ0",89.4,0.0,"pheA NCTC5050_01083",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[468.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A6TCK5",89.4,0.0,"pheA KPN_02920",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[469.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A0A0H3GTV9",89.4,0.0,"KPHS_39900",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[470.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A0A378EB22",94.1,3.899999999999999E-72,"pheA_2 NCTC5046_04703",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[471.0,"5.4.99.5","P-protein","Escherichia coli (strain K12)","P0A9J8","BE0004360","A0A378EAY2",88.5,6.699999999999998E-84,"pheA_1 pheA NCTC5046_04702","Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O; Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51; Evidence={ECO:0000256|RuleBase:RU361254};",null,"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[472.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A0H3GJ91",91.7,0.0,"murE KPHS_08050","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[473.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A0H3GJ91",91.7,0.0,"murE KPHS_08050","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[474.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A0H3GJ91",91.7,0.0,"murE KPHS_08050","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[475.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A6T4M8",91.7,0.0,"murE KPN_00089","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[476.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A6T4M8",91.7,0.0,"murE KPN_00089","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[477.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A6T4M8",91.7,0.0,"murE KPN_00089","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[478.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378EC10",91.7,0.0,"murE NCTC5046_04264","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[479.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378EC10",91.7,0.0,"murE NCTC5046_04264","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[480.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378EC10",91.7,0.0,"murE NCTC5046_04264","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[481.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378C1F3",91.9,0.0,"murE NCTC5050_06625","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[482.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378C1F3",91.9,0.0,"murE NCTC5050_06625","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[483.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","A0A378C1F3",91.9,0.0,"murE NCTC5050_06625","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[484.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A0A0H3GI71",67.9,0.0,"murC KPHS_08120","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[485.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A0A0H3GI71",67.9,0.0,"murC KPHS_08120","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[486.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A0A0H3GI71",67.9,0.0,"murC KPHS_08120","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[487.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A6T4N4",67.9,0.0,"murC KPN78578_00940 KPN_00095","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[488.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A6T4N4",67.9,0.0,"murC KPN78578_00940 KPN_00095","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[489.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","A6T4N4",67.9,0.0,"murC KPN78578_00940 KPN_00095","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[490.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[491.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[492.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[493.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[494.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[495.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[496.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[497.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378C1D3",88.4,0.0,"murD NCTC5050_06622","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[498.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[499.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[500.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[501.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[502.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[503.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[504.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[505.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A378E9W8",88.6,0.0,"murD NCTC5046_04267","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[506.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[507.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[508.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[509.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[510.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[511.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[512.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[513.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A0A0H3GML0",89.0,0.0,"murD KPHS_08080","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[514.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[515.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[516.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[517.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[518.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[519.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[520.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[521.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","A6T4N1",89.0,0.0,"murD KPN_00092","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382010}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01124339};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[522.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[523.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[524.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[525.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[526.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[527.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[528.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[529.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[530.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[531.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[532.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378E671",96.3,0.0,"accC NCTC5046_02598","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[533.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[534.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[535.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[536.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[537.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[538.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[539.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[540.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[541.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[542.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[543.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A0H3GTW5",96.7,0.0,"KPHS_47970","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[544.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[545.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[546.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[547.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[548.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[549.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[550.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[551.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[552.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[553.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[554.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A6TES3",96.7,0.0,"accC KPN_03665","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[555.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[556.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[557.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[558.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[559.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[560.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[561.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[562.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[563.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[564.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[565.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","A0A378ALU9",96.6,0.0,"accC NCTC5050_02528","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[566.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A6TH93",95.4,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[567.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A6TH93",95.4,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[568.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A6TH93",95.4,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[569.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A0H3GLD4",95.4,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[570.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A0H3GLD4",95.4,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[571.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A0H3GLD4",95.4,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[572.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A378AZ23",95.1,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[573.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A378AZ23",95.1,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[574.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","A0A378AZ23",95.1,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[575.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","A0A378AZ23",89.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[576.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","A6TH93",89.4,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[577.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","A0A0H3GLD4",89.4,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[578.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02109","Hadacidin","experimental","unknown"]
[579.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[580.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[581.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[582.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[583.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[584.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[585.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[586.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A378AZ23",95.4,0.0,"purA NCTC5050_03719","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[587.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02109","Hadacidin","experimental","unknown"]
[588.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[589.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[590.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[591.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[592.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[593.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[594.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[595.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A0A0H3GLD4",95.6,0.0,"purA KPHS_04230","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[596.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[597.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[598.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[599.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[600.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[601.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[602.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[603.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[604.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","A6TH93",95.6,0.0,"purA KPN78578_45030 KPN_04576","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[605.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","A0A377Z7K9",95.1,0.0,"guaA_1 NCTC5050_01199","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000256|SAAS:SAAS01124569};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[606.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","A0A378EBK9",95.8,0.0,"guaA_1 guaA NCTC5046_04830","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS00723675}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS01117722};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[607.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","A0A0H3GRL9",96.0,0.0,"guaA KPHS_39070","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS00723675}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS01117722};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[608.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","A6TCC2",96.0,0.0,"guaA KPN78578_27820 KPN_02833","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-Rule:MF_00344}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00344};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"H.influenzae FBA-only","index":2,"n_rows":49,"n_cols":19,"rows_kept":49,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB06847","5-[(3S)-3-(2-methoxybiphenyl-4-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[1.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07140","5-[(3R)-3-(5-methoxybiphenyl-3-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[2.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07142","5-[(3R)-3-(5-methoxy-3',5'-dimethylbiphenyl-3-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[3.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07153","6-methyl-5-[3-methyl-3-(3,4,5-trimethoxyphenyl)but-1-yn-1-yl]pyrimidine-2,4-diamine","experimental","unknown"]
[4.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[5.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","P43791",44.1,1.6E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07938","5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-chroman-5-yl]methyl]pyrimidine-2,4-diamine","experimental","unknown"]
[6.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","P43791",44.1,1.6E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[7.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","P43791",44.1,1.6E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB08741","5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-2H-chromen-5-yl]methyl]pyrimidine-2,4-diamine","experimental","unknown"]
[8.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[9.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[10.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB11596","Levoleucovorin","approved","unknown"]
[11.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[12.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB12769","Lometrexol","investigational","unknown"]
[13.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB03904","Urea","approved","unknown"]
[14.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[15.0,"1.8.1.4","Outer membrane protein p64k or PM-6","Neisseria meningitidis","Q51225","BE0002980","P43784",63.1,0.0,"lpdA HI_1231",null,"FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4;",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[16.0,"2.4.2.8","Hypoxanthine phosphoribosyltransferase","Escherichia coli (strain K12)","P0A9M2","BE0002080","P45078",69.1,1.0999999999999998E-79,"hpt HI_1153","Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1. ","FUNCTION: Acts preferentially on hypoxanthine; has very low activity towards guanine. Inactive towards xanthine (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8;",null,"DB04566","Inosinic Acid","experimental","unknown"]
[17.0,"2.5.1.27","Adenylate dimethylallyltransferase","Agrobacterium tumefaciens (strain C58 / ATCC 33970)","P58758","BE0004050","P44495",25.6,1.9,"miaA trpX HI_0068",null,"FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). {ECO:0000255|HAMAP-Rule:MF_00185}.","CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA; Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411, ChEBI:CHEBI:74415; EC=2.5.1.75; Evidence={ECO:0000255|HAMAP-Rule:MF_00185};",null,"DB02270","Dimethylallyl S-Thiolodiphosphate","experimental","unknown"]
[18.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","P44920",48.8,1.8E-60,"coaE HI_0890","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24;","1JJV;","DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[19.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","P24323",71.5,1.8999999999999998E-109,"adk HI_0349","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity). It may be linked to the biosynthesis of lipopolysaccharide surface molecules, which are important for the pathogenesis of H.influenzae. {ECO:0000255|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[20.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","P44719",62.2,6.899999999999999E-85,"tmk HI_0456",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[21.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB04610","7,8-dihydro-6-hydroxymethyl-7-methyl-7-[2-phenylethyl]-pterin","experimental","unknown"]
[22.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB04158","6-(Adenosine Tetraphosphate-Methyl)-7,8-Dihydropterin","experimental","unknown"]
[23.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB04047","[Pterin-6-Yl Methanyl]-Phosphonophosphate","experimental","unknown"]
[24.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[25.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB02119","6-Hydroxymethyl-7,8-Dihydropterin","experimental","unknown"]
[26.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB03197","6-Hydroxymethylpterin","experimental","unknown"]
[27.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43777","BE0001488","P43777",100.0,5.2999999999999994E-110,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB02278","7,8-Dihydro-7,7-Dimethyl-6-Hydroxypterin","experimental","unknown"]
[28.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","P44490",100.0,8.899999999999998E-178,"kdsB HI_0058","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};","1VH3;1VIC;3DUV;","DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[29.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB04015","Methionine Phosphinate","experimental","unknown"]
[30.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB03816","Difluoromethionine","experimental","unknown"]
[31.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB03799","Trifluoromethionine","experimental","unknown"]
[32.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB02229","5'-O-[(L-Methionyl)-Sulphamoyl]Adenosine","experimental","unknown"]
[33.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB02151","Methionine Phosphonate","experimental","unknown"]
[34.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB00150","L-Tryptophan","approved, nutraceutical, withdrawn","unknown","substrateinhibitor"]
[35.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB04537","L-Tryptophanamide","experimental","unknown"]
[36.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[37.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB00150","L-Tryptophan","approved, nutraceutical, withdrawn","unknown","inhibitor"]
[38.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB01831","Tryptophanyl-5'amp","experimental","unknown"]
[39.0,"6.1.1.21","Histidine--tRNA ligase","Escherichia coli (strain K12)","P60906","BE0001795","P43823",66.8,0.0,"hisS HI_0369",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;",null,"DB03811","Histidinol","experimental","unknown"]
[40.0,"6.1.1.21","Histidine--tRNA ligase","Escherichia coli (strain K12)","P60906","BE0001795","P43823",66.8,0.0,"hisS HI_0369",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;",null,"DB04201","Histidyl-Adenosine Monophosphate","experimental","unknown"]
[41.0,"6.1.1.3","Threonine--tRNA ligase","Shigella flexneri","P0A8M5","BE0001579","P43014",78.0,0.0,"thrS HI_1367",null,"FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-Rule:MF_00184}.","CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00184};",null,"DB04024","N'-L-Seryl-3'-Amino-(3'-Deoxy)-Adenosine","experimental","unknown"]
[42.0,"6.1.1.3","Threonine--tRNA ligase","Shigella flexneri","P0A8M5","BE0001579","P43014",78.0,0.0,"thrS HI_1367",null,"FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-Rule:MF_00184}.","CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00184};",null,"DB03869","5'-O-(N-(L-Seryl)-Sulfamoyl)Adenosine","experimental","unknown"]
[43.0,"6.1.1.3","Threonine--tRNA ligase","Shigella flexneri","P0A8M5","BE0001579","P43014",78.0,0.0,"thrS HI_1367",null,"FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-Rule:MF_00184}.","CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00184};",null,"DB03355","5'-O-(N-(L-Threonyl)-Sulfamoyl)Adenosine","experimental","unknown"]
[44.0,"6.2.1.22","[Citrate [pro-3S]-lyase] ligase","Escherichia coli (strain K12)","P77390","BE0000805","P44462",52.9,1.3999999999999997E-115,"citC HI_0025",null,"FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.","CATALYTIC ACTIVITY: Reaction=acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate; Xref=Rhea:RHEA:23788, Rhea:RHEA-COMP:10158, Rhea:RHEA-COMP:13710, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82683, ChEBI:CHEBI:137976, ChEBI:CHEBI:456215; EC=6.2.1.22;",null,"DB00336","Nitrofural","approved, investigational, vet_approved","yes","inhibitor"]
[45.0,"6.3.4.5","Argininosuccinate synthase","Escherichia coli (strain K12)","P0A6E4","BE0001754","P44315",79.2,0.0,"argG HI_1727","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5;",null,"DB00536","Guanidine","approved","unknown"]
[46.0,"6.3.4.5","Argininosuccinate synthase","Escherichia coli (strain K12)","P0A6E4","BE0001754","P44315",79.2,0.0,"argG HI_1727","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5;",null,"DB09462","Glycerin","approved, investigational","unknown"]
[47.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","P44335",78.2,0.0,"guaA HI_0222","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"H.influenzae FBA+FVA","index":3,"n_rows":49,"n_cols":19,"rows_kept":49,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB06847","5-[(3S)-3-(2-methoxybiphenyl-4-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[1.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07140","5-[(3R)-3-(5-methoxybiphenyl-3-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[2.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07142","5-[(3R)-3-(5-methoxy-3',5'-dimethylbiphenyl-3-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[3.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07153","6-methyl-5-[3-methyl-3-(3,4,5-trimethoxyphenyl)but-1-yn-1-yl]pyrimidine-2,4-diamine","experimental","unknown"]
[4.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","P43791",43.8,8.4E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[5.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","P43791",44.1,1.6E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07938","5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-chroman-5-yl]methyl]pyrimidine-2,4-diamine","experimental","unknown"]
[6.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","P43791",44.1,1.6E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[7.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","P43791",44.1,1.6E-36,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB08741","5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-2H-chromen-5-yl]methyl]pyrimidine-2,4-diamine","experimental","unknown"]
[8.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[9.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[10.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB11596","Levoleucovorin","approved","unknown"]
[11.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[12.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB12769","Lometrexol","investigational","unknown"]
[13.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB03904","Urea","approved","unknown"]
[14.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","P43791",53.5,1.3000000000000001E-52,"folA folH HI_0899","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[15.0,"1.8.1.4","Outer membrane protein p64k or PM-6","Neisseria meningitidis","Q51225","BE0002980","P43784",63.1,0.0,"lpdA HI_1231",null,"FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4;",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[16.0,"2.4.2.8","Hypoxanthine phosphoribosyltransferase","Escherichia coli (strain K12)","P0A9M2","BE0002080","P45078",69.1,1.0999999999999998E-79,"hpt HI_1153","Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1. ","FUNCTION: Acts preferentially on hypoxanthine; has very low activity towards guanine. Inactive towards xanthine (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8;",null,"DB04566","Inosinic Acid","experimental","unknown"]
[17.0,"2.5.1.27","Adenylate dimethylallyltransferase","Agrobacterium tumefaciens (strain C58 / ATCC 33970)","P58758","BE0004050","P44495",25.6,1.9,"miaA trpX HI_0068",null,"FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). {ECO:0000255|HAMAP-Rule:MF_00185}.","CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA; Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411, ChEBI:CHEBI:74415; EC=2.5.1.75; Evidence={ECO:0000255|HAMAP-Rule:MF_00185};",null,"DB02270","Dimethylallyl S-Thiolodiphosphate","experimental","unknown"]
[18.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","P44920",48.8,1.8E-60,"coaE HI_0890","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24;","1JJV;","DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[19.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","P24323",71.5,1.8999999999999998E-109,"adk HI_0349","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity). It may be linked to the biosynthesis of lipopolysaccharide surface molecules, which are important for the pathogenesis of H.influenzae. {ECO:0000255|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[20.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","P44719",62.2,6.899999999999999E-85,"tmk HI_0456",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;",null,"DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[21.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB04610","7,8-dihydro-6-hydroxymethyl-7-methyl-7-[2-phenylethyl]-pterin","experimental","unknown"]
[22.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB04158","6-(Adenosine Tetraphosphate-Methyl)-7,8-Dihydropterin","experimental","unknown"]
[23.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB04047","[Pterin-6-Yl Methanyl]-Phosphonophosphate","experimental","unknown"]
[24.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[25.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB02119","6-Hydroxymethyl-7,8-Dihydropterin","experimental","unknown"]
[26.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","P43777",56.3,1.1E-58,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB03197","6-Hydroxymethylpterin","experimental","unknown"]
[27.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43777","BE0001488","P43777",100.0,5.2999999999999994E-110,"folK HI_0064","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;","1CBK;","DB02278","7,8-Dihydro-7,7-Dimethyl-6-Hydroxypterin","experimental","unknown"]
[28.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","P44490",100.0,8.899999999999998E-178,"kdsB HI_0058","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};","1VH3;1VIC;3DUV;","DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[29.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB04015","Methionine Phosphinate","experimental","unknown"]
[30.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB03816","Difluoromethionine","experimental","unknown"]
[31.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB03799","Trifluoromethionine","experimental","unknown"]
[32.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB02229","5'-O-[(L-Methionyl)-Sulphamoyl]Adenosine","experimental","unknown"]
[33.0,"6.1.1.10","Methionine--tRNA ligase","Escherichia coli (strain K12)","P00959","BE0001537","P43828",68.3,0.0,"metG HI_1276",null,"FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.","CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};",null,"DB02151","Methionine Phosphonate","experimental","unknown"]
[34.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB00150","L-Tryptophan","approved, nutraceutical, withdrawn","unknown","substrateinhibitor"]
[35.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB04537","L-Tryptophanamide","experimental","unknown"]
[36.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[37.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB00150","L-Tryptophan","approved, nutraceutical, withdrawn","unknown","inhibitor"]
[38.0,"6.1.1.2","Tryptophan--tRNA ligase","Geobacillus stearothermophilus","P00953","BE0001343","P43835",54.6,1.3999999999999997E-116,"trpS HI_0637",null,"FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). {ECO:0000255|HAMAP-Rule:MF_00140}.","CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00140};","6DFU;","DB01831","Tryptophanyl-5'amp","experimental","unknown"]
[39.0,"6.1.1.21","Histidine--tRNA ligase","Escherichia coli (strain K12)","P60906","BE0001795","P43823",66.8,0.0,"hisS HI_0369",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;",null,"DB03811","Histidinol","experimental","unknown"]
[40.0,"6.1.1.21","Histidine--tRNA ligase","Escherichia coli (strain K12)","P60906","BE0001795","P43823",66.8,0.0,"hisS HI_0369",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;",null,"DB04201","Histidyl-Adenosine Monophosphate","experimental","unknown"]
[41.0,"6.1.1.3","Threonine--tRNA ligase","Shigella flexneri","P0A8M5","BE0001579","P43014",78.0,0.0,"thrS HI_1367",null,"FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-Rule:MF_00184}.","CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00184};",null,"DB04024","N'-L-Seryl-3'-Amino-(3'-Deoxy)-Adenosine","experimental","unknown"]
[42.0,"6.1.1.3","Threonine--tRNA ligase","Shigella flexneri","P0A8M5","BE0001579","P43014",78.0,0.0,"thrS HI_1367",null,"FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-Rule:MF_00184}.","CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00184};",null,"DB03869","5'-O-(N-(L-Seryl)-Sulfamoyl)Adenosine","experimental","unknown"]
[43.0,"6.1.1.3","Threonine--tRNA ligase","Shigella flexneri","P0A8M5","BE0001579","P43014",78.0,0.0,"thrS HI_1367",null,"FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-Rule:MF_00184}.","CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00184};",null,"DB03355","5'-O-(N-(L-Threonyl)-Sulfamoyl)Adenosine","experimental","unknown"]
[44.0,"6.2.1.22","[Citrate [pro-3S]-lyase] ligase","Escherichia coli (strain K12)","P77390","BE0000805","P44462",52.9,1.3999999999999997E-115,"citC HI_0025",null,"FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.","CATALYTIC ACTIVITY: Reaction=acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate; Xref=Rhea:RHEA:23788, Rhea:RHEA-COMP:10158, Rhea:RHEA-COMP:13710, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82683, ChEBI:CHEBI:137976, ChEBI:CHEBI:456215; EC=6.2.1.22;",null,"DB00336","Nitrofural","approved, investigational, vet_approved","yes","inhibitor"]
[45.0,"6.3.4.5","Argininosuccinate synthase","Escherichia coli (strain K12)","P0A6E4","BE0001754","P44315",79.2,0.0,"argG HI_1727","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5;",null,"DB00536","Guanidine","approved","unknown"]
[46.0,"6.3.4.5","Argininosuccinate synthase","Escherichia coli (strain K12)","P0A6E4","BE0001754","P44315",79.2,0.0,"argG HI_1727","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5;",null,"DB09462","Glycerin","approved, investigational","unknown"]
[47.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","P44335",78.2,0.0,"guaA HI_0222","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"P.aeruginosa PA14 FBA-only","index":4,"n_rows":179,"n_cols":19,"rows_kept":179,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.100","3-oxoacyl-[acyl-carrier-protein] reductase FabG","Escherichia coli (strain K12)","P0AEK2","BE0002069","O54438",64.2,3.699999999999999E-101,"fabG PA2967","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;","4AFN;4AG3;4BNT;4BNU;4BNV;4BNW;4BNX;4BNY;4BNZ;4BO0;4BO1;4BO2;4BO3;4BO4;4BO5;4BO6;4BO7;4BO8;4BO9;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[1.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[2.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[3.0,"1.1.1.25","Shikimate dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43876","BE0001445","P43904",44.5,8.100000000000001E-61,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[4.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB02496","1-Deoxy-D-xylulose 5-phosphate","experimental","unknown"]
[5.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB02948","Fosmidomycin","experimental, investigational","unknown"]
[6.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB03649","[{(5-Chloro-2-Pyridinyl)Amino} Methylene]-1,1-Bisphosphonate","experimental","unknown"]
[7.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[8.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[9.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB04267","Dipicolinic Acid","experimental","unknown"]
[10.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","Q51344",67.0,0.0,"asd PA3117","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000269|PubMed:12071715}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000269|PubMed:12071715};","5BNT;","DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[11.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","Q51344",67.0,0.0,"asd PA3117","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000269|PubMed:12071715}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000269|PubMed:12071715};","5BNT;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[12.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","Q51344",67.0,0.0,"asd PA3117","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000269|PubMed:12071715}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000269|PubMed:12071715};","5BNT;","DB04498","Aspartate Semialdehyde","experimental","unknown"]
[13.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[14.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[15.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[16.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[17.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved","unknown"]
[18.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved","unknown"]
[19.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[20.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[21.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[22.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB04007","Bromo-WR99210","experimental","unknown"]
[23.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB00951","Isoniazid","approved","unknown"]
[24.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[25.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[26.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[27.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[28.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[29.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[30.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[31.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[32.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[33.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[34.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[35.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[36.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[37.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[38.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[39.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[40.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[41.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[42.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[43.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[44.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[45.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[46.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[47.0,"2.2.1.1","Transketolase 1","Escherichia coli (strain K12)","P27302","BE0003276","Q9I5Y8",73.0,0.0,"tktA PA0548",null,"FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.","CATALYTIC ACTIVITY: ; Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1; Evidence={ECO:0000256|RuleBase:RU004996};","4XEU;","DB01987","Cocarboxylase","approved, experimental","unknown"]
[48.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[49.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[50.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[51.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[52.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[53.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[54.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[55.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[56.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","Q9HW01",44.8,8.099999999999999E-90,"murG PA4412","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: ; Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};","3S2U;","DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[57.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[58.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[59.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[60.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[61.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[62.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02270","Dimethylallyl S-Thiolodiphosphate","experimental","unknown"]
[63.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02508","Isopentyl Pyrophosphate","experimental","unknown"]
[64.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[65.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[66.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[67.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[68.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[69.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[70.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[71.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[72.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[73.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[74.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[75.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[76.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[77.0,"2.5.1.61","Porphobilinogen deaminase","Escherichia coli (strain K12)","P06983","BE0001758","Q60169",67.8,1.0999999999999998E-138,"hemC PA5260","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. ","FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+); Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;",null,"DB04517","Dipyrromethane Cofactor","experimental","unknown"]
[78.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[79.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[80.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[81.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[82.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[83.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[84.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[85.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[86.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[87.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[88.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[89.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[90.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[91.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q9I2Y1",47.5,8.199999999999996E-121,"pabB PA1758",{"$nulls":4},"DB01942","Formic Acid","approved, experimental","unknown"]
[92.0,"2.7.1.148","4-diphosphocytidyl-2-C-methyl-D-erythritol kinase","Shigella flexneri","Q83LD8","BE0001574","P42805",54.6,2.9999999999999992E-99,"ispE PA4669","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. ","FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823, ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148; Evidence={ECO:0000255|HAMAP-Rule:MF_00061};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[93.0,"2.7.1.148","4-diphosphocytidyl-2-C-methyl-D-erythritol kinase","Shigella flexneri","Q83LD8","BE0001574","P42805",54.6,2.9999999999999992E-99,"ispE PA4669","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. ","FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823, ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148; Evidence={ECO:0000255|HAMAP-Rule:MF_00061};",null,"DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[94.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[95.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[96.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[97.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[98.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","Q9HXV4",64.4,1.6999999999999996E-91,"adk PA3686","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: ; Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[99.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q9HT22",53.0,1.9999999999999995E-166,"glmU PA5552","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: ; Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};; CATALYTIC ACTIVITY: ; Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[100.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[101.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[102.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB03854","Pentane-1,5-Diamine","experimental","unknown"]
[103.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[104.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[105.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[106.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[107.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase","Actinomadura sp. (strain R39)","P39045","BE0003356","Q9HZG1",29.4,3.7E-32,"PA3047",{"$nulls":4},"DB04742","(2R)-2-{(1R)-2-oxo-1-[(2-thienylacetyl)amino]ethyl}-5,6-dihydro-2h-1,3-thiazine-4-carboxylic acid","experimental","unknown"]
[108.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00274","Cefmetazole","approved, investigational","yes","inhibitor"]
[109.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00303","Ertapenem","approved, investigational","yes","inhibitor"]
[110.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00430","Cefpiramide","approved","yes","inhibitor"]
[111.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB01331","Cefoxitin","approved","yes","inhibitor"]
[112.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB01329","Cefoperazone","approved, investigational","yes","inhibitor"]
[113.0,"3.4.16.4","Peptidoglycan synthase FtsI","Escherichia coli O157:H7","P0AD69","BE0003396","G3XD46",45.1,9.599999999999997E-158,"ftsI pbpB PA4418","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:20580675). {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:20580675}.","CATALYTIC ACTIVITY: ; Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-Rule:MF_02080};","3PBN;3PBO;3PBQ;3PBR;3PBS;3PBT;4KQO;4KQQ;4KQR;","DB05659","faropenem medoxomil","investigational","unknown"]
[114.0,"3.4.16.4","Peptidoglycan synthase FtsI","Escherichia coli O157:H7","P0AD69","BE0003396","Q9I1K1",41.6,3.499999999999999E-131,"pbpC PA2272","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:9045804). {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:9045804}.","CATALYTIC ACTIVITY: ; Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-Rule:MF_02080};",null,"DB05659","faropenem medoxomil","investigational","unknown"]
[115.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","P0AEB3","BE0002475","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB04647","BOC-GAMMA-D-GLU-L-LYS(CBZ)-D-BOROALA","experimental","unknown"]
[116.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","P0AEB3","BE0002475","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01147","Cloxacillin","approved, vet_approved","unknown","inhibitor"]
[117.0,"3.4.16.4","Penicillin-binding protein","Gram positive and gram negative bacteria","P0AEB2","BE0004840","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB09319","Carindacillin","approved, investigational","yes","inhibitor"]
[118.0,"3.4.16.4","Penicillin-binding protein","Gram positive and gram negative bacteria","P0AEB2","BE0004840","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB00578","Carbenicillin","approved, investigational","yes","inhibitor"]
[119.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[120.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[121.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[122.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[123.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[124.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[125.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q9HZN6",35.8,1.6E-36,"pabC PA2964",null,null,null,"2Y4R;","DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[126.0,"4.1.3.40","Chorismate--pyruvate lyase","Escherichia coli (strain K12)","P26602","BE0001507","Q9HTK1",31.4,4.7E-13,"ubiC PA5357","Cofactor biosynthesis; ubiquinone biosynthesis. ","FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = 4-hydroxybenzoate + pyruvate; Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879, ChEBI:CHEBI:29748; EC=4.1.3.40; Evidence={ECO:0000255|HAMAP-Rule:MF_01632};",null,"DB02130","Vanillic acid","experimental","unknown"]
[127.0,"4.1.3.40","Chorismate--pyruvate lyase","Escherichia coli (strain K12)","P26602","BE0001507","Q9HTK1",31.4,4.7E-13,"ubiC PA5357","Cofactor biosynthesis; ubiquinone biosynthesis. ","FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = 4-hydroxybenzoate + pyruvate; Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879, ChEBI:CHEBI:29748; EC=4.1.3.40; Evidence={ECO:0000255|HAMAP-Rule:MF_01632};",null,"DB04242","P-Hydroxybenzoic Acid","experimental","unknown"]
[128.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB02828","5-Fluorolevulinic Acid","experimental","unknown"]
[129.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB01942","Formic Acid","approved, experimental","unknown"]
[130.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","O33877",68.6,8.399999999999998E-83,"fabA PA1610","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;; CATALYTIC ACTIVITY: ; Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;; CATALYTIC ACTIVITY: ; Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;","4B0B;4B0C;4B0I;4B0J;4B8U;4CL6;4FQ9;","DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[131.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","O33877",68.6,8.399999999999998E-83,"fabA PA1610","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;; CATALYTIC ACTIVITY: ; Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;; CATALYTIC ACTIVITY: ; Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;","4B0B;4B0C;4B0I;4B0J;4B8U;4CL6;4FQ9;","DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[132.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","Q9I344",43.2,1.1E-96,"aroC PA1681","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: ; Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[133.0,"4.3.3.7","4-hydroxy-tetrahydrodipicolinate synthase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X1K9","BE0001460","Q9I4W3",44.4,1.2999999999999997E-80,"dapA PA1010","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. ","FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). {ECO:0000305|PubMed:21396954}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00418};","3NOE;3PS7;3PUO;3QZE;3S8H;","DB02370","Nz-(1-Carboxyethyl)-Lysine","experimental","unknown"]
[134.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Escherichia coli (strain K12)","P62617","BE0004106","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[135.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shewanella oneidensis (strain MR-1)","Q8EBR3","BE0004091","P57708",68.2,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB07780","FARNESYL DIPHOSPHATE","experimental","unknown"]
[136.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[137.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[138.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03961","2c-Methyl-D-Erythritol 2,4-Cyclodiphosphate","experimental","unknown"]
[139.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[140.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[141.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB01859","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol 2-Phosphate","experimental","unknown"]
[142.0,"5.3.1.1","Triosephosphate isomerase","Vibrio marinus","P50921","BE0001889","Q9HV51",50.4,7.2E-76,"tpiA PA4748","Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. ","FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.","CATALYTIC ACTIVITY: ; Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};",null,"DB02726","2-Phosphoglycolic Acid","experimental","unknown"]
[143.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","Q9I6G1",57.7,1.1999999999999998E-80,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[144.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","Q9I6G1",64.3,1.2999999999999998E-89,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[145.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02843","alpha-D-glucose-1-phosphate","experimental","unknown"]
[146.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB04522","Dexfosfoserine","experimental","unknown"]
[147.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02867","D-Mannose 1-Phosphate","experimental","unknown"]
[148.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02900","alpha-D-mannose 6-phosphate","experimental","unknown"]
[149.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[150.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[151.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[152.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[153.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[154.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[155.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[156.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[157.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[158.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[159.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[160.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[161.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[162.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[163.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[164.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[165.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[166.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[167.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","Q9HUM6",70.9,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[168.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[169.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[170.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[171.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[172.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[173.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[174.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[175.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[176.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[177.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","Q9HXM6",70.9,0.0,"guaA PA3769","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"P.aeruginosa PA14 FBA+FVA","index":5,"n_rows":177,"n_cols":19,"rows_kept":177,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.100","3-oxoacyl-[acyl-carrier-protein] reductase FabG","Escherichia coli (strain K12)","P0AEK2","BE0002069","O54438",64.2,3.699999999999999E-101,"fabG PA2967","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;","4AFN;4AG3;4BNT;4BNU;4BNV;4BNW;4BNX;4BNY;4BNZ;4BO0;4BO1;4BO2;4BO3;4BO4;4BO5;4BO6;4BO7;4BO8;4BO9;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[1.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[2.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[3.0,"1.1.1.25","Shikimate dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43876","BE0001445","P43904",44.5,8.100000000000001E-61,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[4.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[5.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB03649","[{(5-Chloro-2-Pyridinyl)Amino} Methylene]-1,1-Bisphosphonate","experimental","unknown"]
[6.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB02948","Fosmidomycin","experimental, investigational","unknown"]
[7.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB02496","1-Deoxy-D-xylulose 5-phosphate","experimental","unknown"]
[8.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB04267","Dipicolinic Acid","experimental","unknown"]
[9.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[10.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[11.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[12.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB00951","Isoniazid","approved","unknown"]
[13.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB04007","Bromo-WR99210","experimental","unknown"]
[14.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[15.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[16.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[17.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved","unknown"]
[18.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved","unknown"]
[19.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[20.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[21.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[22.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[23.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[24.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[25.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[26.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[27.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[28.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[29.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[30.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[31.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[32.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[33.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[34.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[35.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[36.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[37.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[38.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[39.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[40.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[41.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[42.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[43.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[44.0,"2.2.1.1","Transketolase 1","Escherichia coli (strain K12)","P27302","BE0003276","Q9I5Y8",73.0,0.0,"tktA PA0548",null,"FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.","CATALYTIC ACTIVITY: ; Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1; Evidence={ECO:0000256|RuleBase:RU004996};","4XEU;","DB01987","Cocarboxylase","approved, experimental","unknown"]
[45.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[46.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[47.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[48.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[49.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[50.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[51.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[52.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[53.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","Q9HW01",44.8,8.099999999999999E-90,"murG PA4412","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: ; Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};","3S2U;","DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[54.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[55.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[56.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[57.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[58.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[59.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02508","Isopentyl Pyrophosphate","experimental","unknown"]
[60.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02270","Dimethylallyl S-Thiolodiphosphate","experimental","unknown"]
[61.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[62.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[63.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[64.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[65.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[66.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[67.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[68.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[69.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[70.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[71.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[72.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[73.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[74.0,"2.5.1.61","Porphobilinogen deaminase","Escherichia coli (strain K12)","P06983","BE0001758","Q60169",67.8,1.0999999999999998E-138,"hemC PA5260","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. ","FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+); Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;",null,"DB04517","Dipyrromethane Cofactor","experimental","unknown"]
[75.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[76.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[77.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[78.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[79.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[80.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[81.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[82.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[83.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[84.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[85.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[86.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[87.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[88.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q9I2Y1",47.5,8.199999999999996E-121,"pabB PA1758",{"$nulls":4},"DB01942","Formic Acid","approved, experimental","unknown"]
[89.0,"2.7.1.148","4-diphosphocytidyl-2-C-methyl-D-erythritol kinase","Shigella flexneri","Q83LD8","BE0001574","P42805",54.6,2.9999999999999992E-99,"ispE PA4669","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. ","FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823, ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148; Evidence={ECO:0000255|HAMAP-Rule:MF_00061};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[90.0,"2.7.1.148","4-diphosphocytidyl-2-C-methyl-D-erythritol kinase","Shigella flexneri","Q83LD8","BE0001574","P42805",54.6,2.9999999999999992E-99,"ispE PA4669","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. ","FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823, ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148; Evidence={ECO:0000255|HAMAP-Rule:MF_00061};",null,"DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[91.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[92.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[93.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[94.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[95.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","Q9HXV4",64.4,1.6999999999999996E-91,"adk PA3686","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: ; Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[96.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q9HT22",53.0,1.9999999999999995E-166,"glmU PA5552","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: ; Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};; CATALYTIC ACTIVITY: ; Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[97.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[98.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB03854","Pentane-1,5-Diamine","experimental","unknown"]
[99.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[100.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[101.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[102.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[103.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[104.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB04647","BOC-GAMMA-D-GLU-L-LYS(CBZ)-D-BOROALA","experimental","unknown"]
[105.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01329","Cefoperazone","approved, investigational","yes","inhibitor"]
[106.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01331","Cefoxitin","approved","yes","inhibitor"]
[107.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB00274","Cefmetazole","approved, investigational","yes","inhibitor"]
[108.0,"3.4.16.4","Peptidoglycan synthase FtsI","Escherichia coli O157:H7","P0AD69","BE0003396","G3XD46",45.1,9.599999999999997E-158,"ftsI pbpB PA4418","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:20580675). {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:20580675}.","CATALYTIC ACTIVITY: ; Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-Rule:MF_02080};","3PBN;3PBO;3PBQ;3PBR;3PBS;3PBT;4KQO;4KQQ;4KQR;","DB05659","faropenem medoxomil","investigational","unknown"]
[109.0,"3.4.16.4","Peptidoglycan synthase FtsI","Escherichia coli O157:H7","P0AD69","BE0003396","Q9I1K1",41.6,3.499999999999999E-131,"pbpC PA2272","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:9045804). {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:9045804}.","CATALYTIC ACTIVITY: ; Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-Rule:MF_02080};",null,"DB05659","faropenem medoxomil","investigational","unknown"]
[110.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","P0AEB3","BE0002475","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01147","Cloxacillin","approved, vet_approved","unknown","inhibitor"]
[111.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","P0AEB3","BE0002475","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB04647","BOC-GAMMA-D-GLU-L-LYS(CBZ)-D-BOROALA","experimental","unknown"]
[112.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00303","Ertapenem","approved, investigational","yes","inhibitor"]
[113.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB01329","Cefoperazone","approved, investigational","yes","inhibitor"]
[114.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB01331","Cefoxitin","approved","yes","inhibitor"]
[115.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00430","Cefpiramide","approved","yes","inhibitor"]
[116.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00274","Cefmetazole","approved, investigational","yes","inhibitor"]
[117.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase","Actinomadura sp. (strain R39)","P39045","BE0003356","Q9HZG1",29.4,3.7E-32,"PA3047",{"$nulls":4},"DB04742","(2R)-2-{(1R)-2-oxo-1-[(2-thienylacetyl)amino]ethyl}-5,6-dihydro-2h-1,3-thiazine-4-carboxylic acid","experimental","unknown"]
[118.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[119.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[120.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[121.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[122.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[123.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[124.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q9HZN6",35.8,1.6E-36,"pabC PA2964",null,null,null,"2Y4R;","DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[125.0,"4.1.3.40","Chorismate--pyruvate lyase","Escherichia coli (strain K12)","P26602","BE0001507","Q9HTK1",31.4,4.7E-13,"ubiC PA5357","Cofactor biosynthesis; ubiquinone biosynthesis. ","FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = 4-hydroxybenzoate + pyruvate; Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879, ChEBI:CHEBI:29748; EC=4.1.3.40; Evidence={ECO:0000255|HAMAP-Rule:MF_01632};",null,"DB02130","Vanillic acid","experimental","unknown"]
[126.0,"4.1.3.40","Chorismate--pyruvate lyase","Escherichia coli (strain K12)","P26602","BE0001507","Q9HTK1",31.4,4.7E-13,"ubiC PA5357","Cofactor biosynthesis; ubiquinone biosynthesis. ","FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = 4-hydroxybenzoate + pyruvate; Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879, ChEBI:CHEBI:29748; EC=4.1.3.40; Evidence={ECO:0000255|HAMAP-Rule:MF_01632};",null,"DB04242","P-Hydroxybenzoic Acid","experimental","unknown"]
[127.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB02828","5-Fluorolevulinic Acid","experimental","unknown"]
[128.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB01942","Formic Acid","approved, experimental","unknown"]
[129.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","O33877",68.6,8.399999999999998E-83,"fabA PA1610","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;; CATALYTIC ACTIVITY: ; Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;; CATALYTIC ACTIVITY: ; Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;","4B0B;4B0C;4B0I;4B0J;4B8U;4CL6;4FQ9;","DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[130.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","O33877",68.6,8.399999999999998E-83,"fabA PA1610","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;; CATALYTIC ACTIVITY: ; Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;; CATALYTIC ACTIVITY: ; Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;","4B0B;4B0C;4B0I;4B0J;4B8U;4CL6;4FQ9;","DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[131.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","Q9I344",43.2,1.1E-96,"aroC PA1681","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: ; Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[132.0,"4.3.3.7","4-hydroxy-tetrahydrodipicolinate synthase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X1K9","BE0001460","Q9I4W3",44.4,1.2999999999999997E-80,"dapA PA1010","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. ","FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). {ECO:0000305|PubMed:21396954}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00418};","3NOE;3PS7;3PUO;3QZE;3S8H;","DB02370","Nz-(1-Carboxyethyl)-Lysine","experimental","unknown"]
[133.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shewanella oneidensis (strain MR-1)","Q8EBR3","BE0004091","P57708",68.2,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB07780","FARNESYL DIPHOSPHATE","experimental","unknown"]
[134.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[135.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[136.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03961","2c-Methyl-D-Erythritol 2,4-Cyclodiphosphate","experimental","unknown"]
[137.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[138.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[139.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB01859","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol 2-Phosphate","experimental","unknown"]
[140.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Escherichia coli (strain K12)","P62617","BE0004106","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[141.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","Q9I6G1",57.7,1.1999999999999998E-80,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[142.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","Q9I6G1",64.3,1.2999999999999998E-89,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[143.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB04522","Dexfosfoserine","experimental","unknown"]
[144.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[145.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02900","alpha-D-mannose 6-phosphate","experimental","unknown"]
[146.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02867","D-Mannose 1-Phosphate","experimental","unknown"]
[147.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02843","alpha-D-glucose-1-phosphate","experimental","unknown"]
[148.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[149.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[150.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[151.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[152.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[153.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[154.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[155.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[156.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[157.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[158.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[159.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[160.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[161.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[162.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[163.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[164.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[165.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","Q9HUM6",70.9,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[166.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[167.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[168.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[169.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[170.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[171.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[172.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[173.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[174.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[175.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","Q9HXM6",70.9,0.0,"guaA PA3769","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"P.aeruginosa CCBH4851 Tier2 FBA","index":6,"n_rows":200,"n_cols":19,"rows_kept":200,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.100","3-oxoacyl-[acyl-carrier-protein] reductase FabG","Escherichia coli (strain K12)","P0AEK2","BE0002069","O54438",64.2,3.699999999999999E-101,"fabG PA2967","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;","4AFN;4AG3;4BNT;4BNU;4BNV;4BNW;4BNX;4BNY;4BNZ;4BO0;4BO1;4BO2;4BO3;4BO4;4BO5;4BO6;4BO7;4BO8;4BO9;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[1.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[2.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[3.0,"1.1.1.25","Shikimate dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43876","BE0001445","P43904",44.5,8.100000000000001E-61,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[4.0,"1.1.1.85","3-isopropylmalate dehydrogenase","Thiobacillus ferrooxidans","Q56268","BE0001699","Q51375",61.7,2.0999999999999996E-142,"leuB PA3118","Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. ","FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.","CATALYTIC ACTIVITY: ; Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85;",null,"DB04279","3-Isopropylmalic Acid","experimental","unknown"]
[5.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[6.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB04267","Dipicolinic Acid","experimental","unknown"]
[7.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","Q51344",67.0,0.0,"asd PA3117","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000269|PubMed:12071715}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000269|PubMed:12071715};","5BNT;","DB04498","Aspartate Semialdehyde","experimental","unknown"]
[8.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","Q51344",67.0,0.0,"asd PA3117","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000269|PubMed:12071715}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000269|PubMed:12071715};","5BNT;","DB03502","(4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate","experimental","unknown"]
[9.0,"1.2.1.11","Aspartate-semialdehyde dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44801","BE0001681","Q51344",67.0,0.0,"asd PA3117","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. ","FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000269|PubMed:12071715}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000269|PubMed:12071715};","5BNT;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[10.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[11.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[12.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB04007","Bromo-WR99210","experimental","unknown"]
[13.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB00951","Isoniazid","approved","unknown"]
[14.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[15.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[16.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[17.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved","unknown"]
[18.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[19.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[20.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved","unknown"]
[21.0,"2.1.1.13","Methionine synthase","Escherichia coli (strain K12)","P13009","BE0001615","Q9I2Q2",67.7,0.0,"metH PA1843","Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. ","FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13;",null,"DB03614","Methylcobalamin","approved, experimental","unknown"]
[22.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[23.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[24.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[25.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[26.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[27.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[28.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[29.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[30.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[31.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[32.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[33.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[34.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[35.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[36.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[37.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[38.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[39.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[40.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[41.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[42.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[43.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[44.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[45.0,"2.2.1.1","Transketolase 1","Escherichia coli (strain K12)","P27302","BE0003276","Q9I5Y8",73.0,0.0,"tktA PA0548",null,"FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.","CATALYTIC ACTIVITY: ; Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1; Evidence={ECO:0000256|RuleBase:RU004996};","4XEU;","DB01987","Cocarboxylase","approved, experimental","unknown"]
[46.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB02327","Triethylene glycol","experimental","unknown"]
[47.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB03361","2-{(9as)-9a-[(1s)-1-Hydroxyethyl]-2,7-Dimethyl-9a,10-Dihydro-5h-Pyrimido[4,5-D][1,3]Thiazolo[3,2-a]Pyrimidin-8-Yl}Ethyl Trihydrogen Diphosphate","experimental","unknown"]
[48.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB01987","Cocarboxylase","approved, experimental","unknown"]
[49.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[50.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[51.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[52.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[53.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[54.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[55.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[56.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[57.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","Q9HW01",44.8,8.099999999999999E-90,"murG PA4412","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: ; Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};","3S2U;","DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[58.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[59.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[60.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[61.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[62.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[63.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02508","Isopentyl Pyrophosphate","experimental","unknown"]
[64.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[65.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02270","Dimethylallyl S-Thiolodiphosphate","experimental","unknown"]
[66.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[67.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[68.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[69.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[70.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[71.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[72.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[73.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[74.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[75.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[76.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[77.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[78.0,"2.5.1.61","Porphobilinogen deaminase","Escherichia coli (strain K12)","P06983","BE0001758","Q60169",67.8,1.0999999999999998E-138,"hemC PA5260","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. ","FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+); Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;",null,"DB04517","Dipyrromethane Cofactor","experimental","unknown"]
[79.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[80.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[81.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[82.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[83.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[84.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[85.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[86.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[87.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[88.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[89.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[90.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[91.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[92.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q9I2Y1",47.5,8.199999999999996E-121,"pabB PA1758",{"$nulls":4},"DB01942","Formic Acid","approved, experimental","unknown"]
[93.0,"2.7.1.148","4-diphosphocytidyl-2-C-methyl-D-erythritol kinase","Shigella flexneri","Q83LD8","BE0001574","P42805",54.6,2.9999999999999992E-99,"ispE PA4669","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. ","FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823, ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148; Evidence={ECO:0000255|HAMAP-Rule:MF_00061};",null,"DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[94.0,"2.7.1.148","4-diphosphocytidyl-2-C-methyl-D-erythritol kinase","Shigella flexneri","Q83LD8","BE0001574","P42805",54.6,2.9999999999999992E-99,"ispE PA4669","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. ","FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823, ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148; Evidence={ECO:0000255|HAMAP-Rule:MF_00061};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[95.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[96.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[97.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[98.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[99.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","Q9HXV4",64.4,1.6999999999999996E-91,"adk PA3686","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: ; Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[100.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q9HT22",53.0,1.9999999999999995E-166,"glmU PA5552","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: ; Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};; CATALYTIC ACTIVITY: ; Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[101.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[102.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB03854","Pentane-1,5-Diamine","experimental","unknown"]
[103.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[104.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[105.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[106.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[107.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[108.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB00274","Cefmetazole","approved, investigational","yes","inhibitor"]
[109.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01331","Cefoxitin","approved","yes","inhibitor"]
[110.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB04647","BOC-GAMMA-D-GLU-L-LYS(CBZ)-D-BOROALA","experimental","unknown"]
[111.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01329","Cefoperazone","approved, investigational","yes","inhibitor"]
[112.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","P0AEB3","BE0002475","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB04647","BOC-GAMMA-D-GLU-L-LYS(CBZ)-D-BOROALA","experimental","unknown"]
[113.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","P0AEB3","BE0002475","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01147","Cloxacillin","approved, vet_approved","unknown","inhibitor"]
[114.0,"3.4.16.4","Peptidoglycan synthase FtsI","Escherichia coli O157:H7","P0AD69","BE0003396","Q9I1K1",41.6,3.499999999999999E-131,"pbpC PA2272","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:9045804). {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:9045804}.","CATALYTIC ACTIVITY: ; Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-Rule:MF_02080};",null,"DB05659","faropenem medoxomil","investigational","unknown"]
[115.0,"3.4.16.4","Peptidoglycan synthase FtsI","Escherichia coli O157:H7","P0AD69","BE0003396","G3XD46",45.1,9.599999999999997E-158,"ftsI pbpB PA4418","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:20580675). {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:20580675}.","CATALYTIC ACTIVITY: ; Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-Rule:MF_02080};","3PBN;3PBO;3PBQ;3PBR;3PBS;3PBT;4KQO;4KQQ;4KQR;","DB05659","faropenem medoxomil","investigational","unknown"]
[116.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase","Actinomadura sp. (strain R39)","P39045","BE0003356","Q9HZG1",29.4,3.7E-32,"PA3047",{"$nulls":4},"DB04742","(2R)-2-{(1R)-2-oxo-1-[(2-thienylacetyl)amino]ethyl}-5,6-dihydro-2h-1,3-thiazine-4-carboxylic acid","experimental","unknown"]
[117.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB01329","Cefoperazone","approved, investigational","yes","inhibitor"]
[118.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB01331","Cefoxitin","approved","yes","inhibitor"]
[119.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00430","Cefpiramide","approved","yes","inhibitor"]
[120.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00274","Cefmetazole","approved, investigational","yes","inhibitor"]
[121.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00303","Ertapenem","approved, investigational","yes","inhibitor"]
[122.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[123.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[124.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[125.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[126.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[127.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[128.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q9HZN6",35.8,1.6E-36,"pabC PA2964",null,null,null,"2Y4R;","DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[129.0,"4.1.3.40","Chorismate--pyruvate lyase","Escherichia coli (strain K12)","P26602","BE0001507","Q9HTK1",31.4,4.7E-13,"ubiC PA5357","Cofactor biosynthesis; ubiquinone biosynthesis. ","FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = 4-hydroxybenzoate + pyruvate; Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879, ChEBI:CHEBI:29748; EC=4.1.3.40; Evidence={ECO:0000255|HAMAP-Rule:MF_01632};",null,"DB04242","P-Hydroxybenzoic Acid","experimental","unknown"]
[130.0,"4.1.3.40","Chorismate--pyruvate lyase","Escherichia coli (strain K12)","P26602","BE0001507","Q9HTK1",31.4,4.7E-13,"ubiC PA5357","Cofactor biosynthesis; ubiquinone biosynthesis. ","FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = 4-hydroxybenzoate + pyruvate; Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879, ChEBI:CHEBI:29748; EC=4.1.3.40; Evidence={ECO:0000255|HAMAP-Rule:MF_01632};",null,"DB02130","Vanillic acid","experimental","unknown"]
[131.0,"4.2.1.20","Tryptophan synthase alpha chain","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","P16608","BE0001719","P07344",41.1,2.7E-54,"trpA PA0035","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00131};",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[132.0,"4.2.1.20","Tryptophan synthase alpha chain","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","P16608","BE0001719","P07344",41.1,2.7E-54,"trpA PA0035","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00131};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[133.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07925","4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[134.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07951","N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID","experimental","unknown"]
[135.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07773","5-FLUOROINDOLE PROPANOL PHOSPHATE","experimental","unknown"]
[136.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07894","4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[137.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[138.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07952","N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID","experimental","unknown"]
[139.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07890","4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID","experimental","unknown"]
[140.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07953","N-[1H-INDOL-3-YL-ACETYL]VALINE ACID","experimental","unknown"]
[141.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07748","2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[142.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07745","2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[143.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07732","2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[144.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB04143","Indole-3-Glycerol Phosphate","experimental","unknown"]
[145.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB02828","5-Fluorolevulinic Acid","experimental","unknown"]
[146.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB01942","Formic Acid","approved, experimental","unknown"]
[147.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","O33877",68.6,8.399999999999998E-83,"fabA PA1610","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;; CATALYTIC ACTIVITY: ; Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;; CATALYTIC ACTIVITY: ; Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;","4B0B;4B0C;4B0I;4B0J;4B8U;4CL6;4FQ9;","DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[148.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","O33877",68.6,8.399999999999998E-83,"fabA PA1610","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;; CATALYTIC ACTIVITY: ; Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;; CATALYTIC ACTIVITY: ; Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;","4B0B;4B0C;4B0I;4B0J;4B8U;4CL6;4FQ9;","DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[149.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","Q9I344",43.2,1.1E-96,"aroC PA1681","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: ; Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[150.0,"4.3.3.7","4-hydroxy-tetrahydrodipicolinate synthase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X1K9","BE0001460","Q9I4W3",44.4,1.2999999999999997E-80,"dapA PA1010","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. ","FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). {ECO:0000305|PubMed:21396954}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00418};","3NOE;3PS7;3PUO;3QZE;3S8H;","DB02370","Nz-(1-Carboxyethyl)-Lysine","experimental","unknown"]
[151.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Escherichia coli (strain K12)","P62617","BE0004106","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[152.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shewanella oneidensis (strain MR-1)","Q8EBR3","BE0004091","P57708",68.2,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB07780","FARNESYL DIPHOSPHATE","experimental","unknown"]
[153.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[154.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[155.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03961","2c-Methyl-D-Erythritol 2,4-Cyclodiphosphate","experimental","unknown"]
[156.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[157.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[158.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB01859","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol 2-Phosphate","experimental","unknown"]
[159.0,"5.3.1.1","Triosephosphate isomerase","Vibrio marinus","P50921","BE0001889","Q9HV51",50.4,7.2E-76,"tpiA PA4748","Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. ","FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.","CATALYTIC ACTIVITY: ; Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};",null,"DB02726","2-Phosphoglycolic Acid","experimental","unknown"]
[160.0,"5.3.1.24","N-(5'-phosphoribosyl)anthranilate isomerase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q56320","BE0001549","Q59649",44.8,2.0E-39,"trpF PA3113","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. ",null,"CATALYTIC ACTIVITY: ; Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24;",null,"DB03543","1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate","experimental","unknown"]
[161.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","Q9I6G1",57.7,1.1999999999999998E-80,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[162.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","Q9I6G1",64.3,1.2999999999999998E-89,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[163.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[164.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02867","D-Mannose 1-Phosphate","experimental","unknown"]
[165.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02900","alpha-D-mannose 6-phosphate","experimental","unknown"]
[166.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02843","alpha-D-glucose-1-phosphate","experimental","unknown"]
[167.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB04522","Dexfosfoserine","experimental","unknown"]
[168.0,"5.4.99.5","Secreted chorismate mutase","Mycobacterium tuberculosis","P9WIB9","BE0004361","Q9HU05",30.3,1.6999999999999998E-12,"aroQ PA5184","Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. ","FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate. The joint presence of this enzyme together with cyclohexadienyl dehydratase and aromatic aminotransferase in the periplasmic compartment comprises a complete three-step chorismate to phenylalanine pathway and accounts for the so called hidden overflow pathway to phenylalanine in P.aeruginosa, in which two possible routes for it exists, namely either via phenylpyruvate or L-arogenate. {ECO:0000250|UniProtKB:P0A9J8, ECO:0000269|PubMed:11532214}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:11532214};",null,"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[169.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[170.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[171.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[172.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[173.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[174.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[175.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[176.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[177.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[178.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[179.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[180.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[181.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[182.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[183.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[184.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[185.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[186.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","Q9HUM6",70.9,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[187.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[188.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[189.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[190.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[191.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[192.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[193.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[194.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[195.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[196.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","Q9HY84",63.1,4.099999999999998E-176,"argG PA3525","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: ; Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00005};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[197.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","Q9HY84",63.1,4.099999999999998E-176,"argG PA3525","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: ; Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00005};",null,"DB02267","Argininosuccinate","experimental","unknown"]
[198.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","Q9HXM6",70.9,0.0,"guaA PA3769","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"Página5","index":7,"n_rows":72,"n_cols":19,"rows_kept":72,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[1.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[2.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[3.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[4.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[5.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[6.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[7.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[8.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[9.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[10.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[11.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[12.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[13.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[14.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[15.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[16.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[17.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[18.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[19.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[20.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[21.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[22.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[23.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB02327","Triethylene glycol","experimental","unknown"]
[24.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB03361","2-{(9as)-9a-[(1s)-1-Hydroxyethyl]-2,7-Dimethyl-9a,10-Dihydro-5h-Pyrimido[4,5-D][1,3]Thiazolo[3,2-a]Pyrimidin-8-Yl}Ethyl Trihydrogen Diphosphate","experimental","unknown"]
[25.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB01987","Cocarboxylase","approved, experimental","unknown"]
[26.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[27.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[28.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[29.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02270","Dimethylallyl S-Thiolodiphosphate","experimental","unknown"]
[30.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02508","Isopentyl Pyrophosphate","experimental","unknown"]
[31.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[32.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[33.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[34.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[35.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[36.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[37.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[38.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[39.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[40.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[41.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[42.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[43.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[44.0,"2.5.1.61","Porphobilinogen deaminase","Escherichia coli (strain K12)","P06983","BE0001758","Q60169",67.8,1.0999999999999998E-138,"hemC PA5260","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. ","FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+); Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;",null,"DB04517","Dipyrromethane Cofactor","experimental","unknown"]
[45.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q9HT22",53.0,1.9999999999999995E-166,"glmU PA5552","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: ; Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};; CATALYTIC ACTIVITY: ; Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[46.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[47.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[48.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[49.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[50.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[51.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[52.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q9HZN6",35.8,1.6E-36,"pabC PA2964",null,null,null,"2Y4R;","DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[53.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB01942","Formic Acid","approved, experimental","unknown"]
[54.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB02828","5-Fluorolevulinic Acid","experimental","unknown"]
[55.0,"4.3.3.7","4-hydroxy-tetrahydrodipicolinate synthase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X1K9","BE0001460","Q9I4W3",44.4,1.2999999999999997E-80,"dapA PA1010","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. ","FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). {ECO:0000305|PubMed:21396954}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00418};","3NOE;3PS7;3PUO;3QZE;3S8H;","DB02370","Nz-(1-Carboxyethyl)-Lysine","experimental","unknown"]
[56.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[57.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[58.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[59.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[60.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[61.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[62.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[63.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[64.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[65.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[66.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[67.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[68.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[69.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[70.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","Q9HXM6",70.9,0.0,"guaA PA3769","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"P.aeruginosa PAO1 2008 FBA-only","index":8,"n_rows":208,"n_cols":19,"rows_kept":208,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.100","3-oxoacyl-[acyl-carrier-protein] reductase FabG","Escherichia coli (strain K12)","P0AEK2","BE0002069","O54438",64.2,3.699999999999999E-101,"fabG PA2967","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;","4AFN;4AG3;4BNT;4BNU;4BNV;4BNW;4BNX;4BNY;4BNZ;4BO0;4BO1;4BO2;4BO3;4BO4;4BO5;4BO6;4BO7;4BO8;4BO9;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[1.0,"1.1.1.133","dTDP-4-dehydrorhamnose reductase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26392","BE0001971","Q9HU23",52.2,3.499999999999999E-97,"rmlD PA5162","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. ","FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. {ECO:0000256|RuleBase:RU364082}.","CATALYTIC ACTIVITY: Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378, ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62830; EC=1.1.1.133; Evidence={ECO:0000256|RuleBase:RU364082};",null,"DB03723","2'-Deoxy-Thymidine-Beta-L-Rhamnose","experimental","unknown"]
[2.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[3.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[4.0,"1.1.1.25","Shikimate dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43876","BE0001445","P43904",44.5,8.100000000000001E-61,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[5.0,"1.1.1.85","3-isopropylmalate dehydrogenase","Thiobacillus ferrooxidans","Q56268","BE0001699","Q51375",61.7,2.0999999999999996E-142,"leuB PA3118","Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. ","FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.","CATALYTIC ACTIVITY: ; Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85;",null,"DB04279","3-Isopropylmalic Acid","experimental","unknown"]
[6.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[7.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB04267","Dipicolinic Acid","experimental","unknown"]
[8.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08265","2-(TOLUENE-4-SULFONYL)-2H-BENZO[D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[9.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01691","Indole Naphthyridinone","experimental","unknown"]
[10.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01865","3-(6-Aminopyridin-3-Yl)-N-Methyl-N-[(1-Methyl-1h-Indol-2-Yl)Methyl]Acrylamide","experimental","unknown"]
[11.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03030","4-(2-Thienyl)-1-(4-Methylbenzyl)-1h-Imidazole","experimental","unknown"]
[12.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03534","3-[(Acetyl-Methyl-Amino)-Methyl]-4-Amino-N-Methyl-N-(1-Methyl-1h-Indol-2-Ylmethyl)-Benzamide","experimental","unknown"]
[13.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB04030","1,3,4,9-Tetrahydro-2-(Hydroxybenzoyl)-9-[(4-Hydroxyphenyl)Methyl]-6-Methoxy-2h-Pyrido[3,4-B]Indole","experimental","unknown"]
[14.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB02379","Beta-D-Glucose","experimental","unknown"]
[15.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08605","6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[16.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08604","Triclosan","approved","unknown"]
[17.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[18.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[19.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB00951","Isoniazid","approved","unknown"]
[20.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB04007","Bromo-WR99210","experimental","unknown"]
[21.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved","unknown"]
[22.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[23.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[24.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[25.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[26.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[27.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved","unknown"]
[28.0,"2.1.1.13","Methionine synthase","Escherichia coli (strain K12)","P13009","BE0001615","Q9I2Q2",67.7,0.0,"metH PA1843","Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. ","FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13;",null,"DB03614","Methylcobalamin","approved, experimental","unknown"]
[29.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[30.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[31.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[32.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[33.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[34.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[35.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[36.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[37.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[38.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[39.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[40.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[41.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[42.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[43.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[44.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[45.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[46.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[47.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[48.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[49.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[50.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[51.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[52.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Escherichia coli (strain K12)","P31057","BE0001744","Q9HV70",50.9,3.399999999999999E-87,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB03795","2-Dehydropantoate","experimental","unknown"]
[53.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Neisseria meningitidis serogroup B (strain MC58)","Q9JZW6","BE0001822","Q9HV70",58.4,2.9999999999999995E-95,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB04074","Alpha-ketoisovalerate","experimental","unknown"]
[54.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB01987","Cocarboxylase","approved, experimental","unknown"]
[55.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB02327","Triethylene glycol","experimental","unknown"]
[56.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB03361","2-{(9as)-9a-[(1s)-1-Hydroxyethyl]-2,7-Dimethyl-9a,10-Dihydro-5h-Pyrimido[4,5-D][1,3]Thiazolo[3,2-a]Pyrimidin-8-Yl}Ethyl Trihydrogen Diphosphate","experimental","unknown"]
[57.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[58.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[59.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[60.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[61.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[62.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[63.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[64.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[65.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","Q9HW01",44.8,8.099999999999999E-90,"murG PA4412","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: ; Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};","3S2U;","DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[66.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[67.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[68.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[69.0,"2.4.2.19","Nicotinate-nucleotide pyrophosphorylase [carboxylating]","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P30012","BE0001347","P30819",57.7,1.6999999999999997E-97,"nadC PA4524","Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1. ","FUNCTION: Involved in the catabolism of quinolinic acid (QA). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate; Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017; EC=2.4.2.19;",null,"DB01796","Quinolinic Acid","experimental","unknown"]
[70.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[71.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[72.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[73.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[74.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[75.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[76.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[77.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[78.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[79.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[80.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[81.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[82.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB01819","Phosphoenolpyruvate","experimental","unknown"]
[83.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[84.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[85.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[86.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[87.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[88.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[89.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[90.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[91.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[92.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[93.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[94.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[95.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[96.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[97.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[98.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[99.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q9I2Y1",47.5,8.199999999999996E-121,"pabB PA1758",{"$nulls":4},"DB01942","Formic Acid","approved, experimental","unknown"]
[100.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","Q9HVP8",52.6,8.900000000000001E-58,"coaE PA4529","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24;",null,"DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[101.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[102.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[103.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04345","7,8-dimethylalloxazine","experimental","unknown"]
[104.0,"2.7.2.8","Acetylglutamate kinase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HTN2","BE0001949","Q9HTN2",100.0,0.0,"argB PA5323","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00082};","2BUF;","DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[105.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[106.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[107.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[108.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[109.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","Q9HZN8",44.1,5.4E-47,"tmk PA2962",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","3UWK;3UWO;3UXM;4E5U;4EDH;4ESH;4GMD;","DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[110.0,"2.7.7.18","Nicotinate-nucleotide adenylyltransferase","Shigella flexneri","P0A753","BE0002611","Q9HX21",39.4,1.4E-39,"nadD PA4006","Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. ","FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18;","1YUL;1YUM;1YUN;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[111.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q9HT22",53.0,1.9999999999999995E-166,"glmU PA5552","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: ; Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};; CATALYTIC ACTIVITY: ; Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[112.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB04485","Deoxythymidine","experimental, investigational","unknown"]
[113.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[114.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB03751","2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose","experimental","unknown"]
[115.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB03723","2'-Deoxy-Thymidine-Beta-L-Rhamnose","experimental","unknown"]
[116.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02843","alpha-D-glucose-1-phosphate","experimental","unknown"]
[117.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[118.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB01643","Thymidine-5'-Phosphate","experimental","unknown"]
[119.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase 2","Shigella flexneri","P61888","BE0001912","Q9HU22",66.0,1.5999999999999997E-135,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[120.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26393","BE0001910","Q9HU22",75.2,2.799999999999999E-159,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB01861","Uridine diphosphate glucose","experimental","unknown"]
[121.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26393","BE0001910","Q9HU22",75.2,2.799999999999999E-159,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[122.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","Q72K87","BE0001943","Q9I6D1",53.9,7.299999999999999E-50,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03912","4'-Phosphopantetheine","experimental","unknown"]
[123.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[124.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03170","Dephospho Coenzyme A","experimental","unknown"]
[125.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03912","4'-Phosphopantetheine","experimental","unknown"]
[126.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","Q9HZM5",54.2,7.4E-86,"kdsB PA2979","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};","4XWI;","DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[127.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[128.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[129.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[130.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[131.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","Q9HVV9",40.1,4.6E-35,"PA4458",null,"FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[132.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q9HWZ6",62.9,1.3E-74,"ppa PA4031",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};","4XEL;","DB06851","N-(pyridin-3-ylmethyl)aniline","experimental","unknown"]
[133.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q9HWZ6",62.9,1.3E-74,"ppa PA4031",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};","4XEL;","DB07291","5-amino-1-(4-chlorophenyl)-1H-pyrazole-4-carbonitrile","experimental","unknown"]
[134.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q9HZN6",35.8,1.6E-36,"pabC PA2964",null,null,null,"2Y4R;","DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[135.0,"4.2.1.20","Tryptophan synthase alpha chain","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","P16608","BE0001719","P07344",41.1,2.7E-54,"trpA PA0035","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00131};",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[136.0,"4.2.1.20","Tryptophan synthase alpha chain","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","P16608","BE0001719","P07344",41.1,2.7E-54,"trpA PA0035","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00131};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[137.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07953","N-[1H-INDOL-3-YL-ACETYL]VALINE ACID","experimental","unknown"]
[138.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07748","2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[139.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07894","4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[140.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07773","5-FLUOROINDOLE PROPANOL PHOSPHATE","experimental","unknown"]
[141.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[142.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07925","4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[143.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07951","N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID","experimental","unknown"]
[144.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07952","N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID","experimental","unknown"]
[145.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB04143","Indole-3-Glycerol Phosphate","experimental","unknown"]
[146.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07732","2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[147.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07745","2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[148.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07890","4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID","experimental","unknown"]
[149.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB02828","5-Fluorolevulinic Acid","experimental","unknown"]
[150.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB01942","Formic Acid","approved, experimental","unknown"]
[151.0,"4.2.1.46","dTDP-glucose 4,6-dehydratase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26391","BE0001740","Q9HU24",61.0,3.5999999999999996E-154,"rmlB PA5161",null,null,"CATALYTIC ACTIVITY: Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477, ChEBI:CHEBI:57649; EC=4.2.1.46; Evidence={ECO:0000256|RuleBase:RU004473};",null,"DB03751","2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose","experimental","unknown"]
[152.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","Q9I344",43.2,1.1E-96,"aroC PA1681","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: ; Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[153.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Mycobacterium tuberculosis","P9WH11","BE0003322","Q9HU21",40.2,7.9E-37,"rmlC PA5164","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000269|PubMed:17046787}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000305|PubMed:17046787};","1RTV;2IXH;2IXI;2IXJ;2IXK;","DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[154.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26394","BE0001669","Q9HU21",65.7,3.899999999999999E-77,"rmlC PA5164","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000269|PubMed:17046787}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000305|PubMed:17046787};","1RTV;2IXH;2IXI;2IXJ;2IXK;","DB02549","3'-O-Acetylthymidine-5'-Diphosphate","experimental","unknown"]
[155.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU21","BE0002506","Q9HU21",100.0,1.7999999999999997E-134,"rmlC PA5164","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000269|PubMed:17046787}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000305|PubMed:17046787};","1RTV;2IXH;2IXI;2IXJ;2IXK;","DB01694","D-tartaric acid","experimental","unknown"]
[156.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","Q9HYQ8",53.8,2.3999999999999995E-104,"hldD rfaD PA3337","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. Bacterial outer membrane biogenesis; LPS core biosynthesis. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[157.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","Q9HYQ8",53.8,2.3999999999999995E-104,"hldD rfaD PA3337","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. Bacterial outer membrane biogenesis; LPS core biosynthesis. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[158.0,"5.3.1.1","Triosephosphate isomerase","Vibrio marinus","P50921","BE0001889","Q9HV51",50.4,7.2E-76,"tpiA PA4748","Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. ","FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.","CATALYTIC ACTIVITY: ; Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};",null,"DB02726","2-Phosphoglycolic Acid","experimental","unknown"]
[159.0,"5.3.1.24","N-(5'-phosphoribosyl)anthranilate isomerase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q56320","BE0001549","Q59649",44.8,2.0E-39,"trpF PA3113","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. ",null,"CATALYTIC ACTIVITY: ; Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24;",null,"DB03543","1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate","experimental","unknown"]
[160.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","Q9HVZ0",100.0,2.0999999999999997E-134,"gmhA PA4425","Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS core biosynthesis. ","FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate; Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203, ChEBI:CHEBI:60204; EC=5.3.1.28;","1X92;3BJZ;","DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[161.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","Q9I6G1",64.3,1.2999999999999998E-89,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[162.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","Q9I6G1",57.7,1.1999999999999998E-80,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[163.0,"5.4.99.5","Secreted chorismate mutase","Mycobacterium tuberculosis","P9WIB9","BE0004361","Q9HU05",30.3,1.6999999999999998E-12,"aroQ PA5184","Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. ","FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate. The joint presence of this enzyme together with cyclohexadienyl dehydratase and aromatic aminotransferase in the periplasmic compartment comprises a complete three-step chorismate to phenylalanine pathway and accounts for the so called hidden overflow pathway to phenylalanine in P.aeruginosa, in which two possible routes for it exists, namely either via phenylpyruvate or L-arogenate. {ECO:0000250|UniProtKB:P0A9J8, ECO:0000269|PubMed:11532214}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:11532214};",null,"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[164.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[165.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03107","Beta-Alanine","experimental","unknown"]
[166.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB01930","2,4-Dihydroxy-3,3-Dimethyl-Butyrate","experimental","unknown"]
[167.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02694","Pantoyl Adenylate","experimental","unknown"]
[168.0,"6.3.2.1","Pantothenate synthetase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","Q5SHF5","BE0004567","Q9HV69",52.6,2.7E-78,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03570","Tris-Hydroxymethyl-Methyl-Ammonium","experimental","unknown"]
[169.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[170.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[171.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[172.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[173.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[174.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[175.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[176.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[177.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[178.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[179.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[180.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[181.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[182.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[183.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[184.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[185.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[186.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[187.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[188.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[189.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[190.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[191.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[192.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[193.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[194.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[195.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[196.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[197.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[198.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[199.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[200.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[201.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[202.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[203.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[204.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[205.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[206.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","Q9HUM6",70.9,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]

{"sheet":"P.aeruginosa PAO1 2008 FBA+FVA","index":9,"n_rows":192,"n_cols":19,"rows_kept":192,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.100","3-oxoacyl-[acyl-carrier-protein] reductase FabG","Escherichia coli (strain K12)","P0AEK2","BE0002069","O54438",64.2,3.699999999999999E-101,"fabG PA2967","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;","4AFN;4AG3;4BNT;4BNU;4BNV;4BNW;4BNX;4BNY;4BNZ;4BO0;4BO1;4BO2;4BO3;4BO4;4BO5;4BO6;4BO7;4BO8;4BO9;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[1.0,"1.1.1.133","dTDP-4-dehydrorhamnose reductase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26392","BE0001971","Q9HU23",52.2,3.499999999999999E-97,"rmlD PA5162","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. ","FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. {ECO:0000256|RuleBase:RU364082}.","CATALYTIC ACTIVITY: Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378, ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62830; EC=1.1.1.133; Evidence={ECO:0000256|RuleBase:RU364082};",null,"DB03723","2'-Deoxy-Thymidine-Beta-L-Rhamnose","experimental","unknown"]
[2.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[3.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[4.0,"1.1.1.25","Shikimate dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43876","BE0001445","P43904",44.5,8.100000000000001E-61,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[5.0,"1.1.1.85","3-isopropylmalate dehydrogenase","Thiobacillus ferrooxidans","Q56268","BE0001699","Q51375",61.7,2.0999999999999996E-142,"leuB PA3118","Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. ","FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.","CATALYTIC ACTIVITY: ; Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85;",null,"DB04279","3-Isopropylmalic Acid","experimental","unknown"]
[6.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[7.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB04267","Dipicolinic Acid","experimental","unknown"]
[8.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01691","Indole Naphthyridinone","experimental","unknown"]
[9.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01865","3-(6-Aminopyridin-3-Yl)-N-Methyl-N-[(1-Methyl-1h-Indol-2-Yl)Methyl]Acrylamide","experimental","unknown"]
[10.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08605","6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[11.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08604","Triclosan","approved","unknown"]
[12.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08265","2-(TOLUENE-4-SULFONYL)-2H-BENZO[D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[13.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB02379","Beta-D-Glucose","experimental","unknown"]
[14.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03030","4-(2-Thienyl)-1-(4-Methylbenzyl)-1h-Imidazole","experimental","unknown"]
[15.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03534","3-[(Acetyl-Methyl-Amino)-Methyl]-4-Amino-N-Methyl-N-(1-Methyl-1h-Indol-2-Ylmethyl)-Benzamide","experimental","unknown"]
[16.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB04030","1,3,4,9-Tetrahydro-2-(Hydroxybenzoyl)-9-[(4-Hydroxyphenyl)Methyl]-6-Methoxy-2h-Pyrido[3,4-B]Indole","experimental","unknown"]
[17.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[18.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[19.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB04007","Bromo-WR99210","experimental","unknown"]
[20.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB00951","Isoniazid","approved","unknown"]
[21.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved","unknown"]
[22.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[23.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[24.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[25.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[26.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[27.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved","unknown"]
[28.0,"2.1.1.13","Methionine synthase","Escherichia coli (strain K12)","P13009","BE0001615","Q9I2Q2",67.7,0.0,"metH PA1843","Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. ","FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13;",null,"DB03614","Methylcobalamin","approved, experimental","unknown"]
[29.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[30.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[31.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[32.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[33.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[34.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[35.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[36.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[37.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[38.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[39.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[40.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[41.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[42.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[43.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[44.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[45.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[46.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[47.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[48.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[49.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[50.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[51.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[52.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Escherichia coli (strain K12)","P31057","BE0001744","Q9HV70",50.9,3.399999999999999E-87,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB03795","2-Dehydropantoate","experimental","unknown"]
[53.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Neisseria meningitidis serogroup B (strain MC58)","Q9JZW6","BE0001822","Q9HV70",58.4,2.9999999999999995E-95,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB04074","Alpha-ketoisovalerate","experimental","unknown"]
[54.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB02327","Triethylene glycol","experimental","unknown"]
[55.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB03361","2-{(9as)-9a-[(1s)-1-Hydroxyethyl]-2,7-Dimethyl-9a,10-Dihydro-5h-Pyrimido[4,5-D][1,3]Thiazolo[3,2-a]Pyrimidin-8-Yl}Ethyl Trihydrogen Diphosphate","experimental","unknown"]
[56.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB01987","Cocarboxylase","approved, experimental","unknown"]
[57.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[58.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[59.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[60.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[61.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[62.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[63.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[64.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[65.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","Q9HW01",44.8,8.099999999999999E-90,"murG PA4412","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: ; Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};","3S2U;","DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[66.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[67.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[68.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[69.0,"2.4.2.19","Nicotinate-nucleotide pyrophosphorylase [carboxylating]","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P30012","BE0001347","P30819",57.7,1.6999999999999997E-97,"nadC PA4524","Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1. ","FUNCTION: Involved in the catabolism of quinolinic acid (QA). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate; Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017; EC=2.4.2.19;",null,"DB01796","Quinolinic Acid","experimental","unknown"]
[70.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[71.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[72.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[73.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[74.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[75.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[76.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[77.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[78.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[79.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB01819","Phosphoenolpyruvate","experimental","unknown"]
[80.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[81.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[82.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[83.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[84.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[85.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[86.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[87.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[88.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[89.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[90.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[91.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[92.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[93.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[94.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[95.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[96.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[97.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[98.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[99.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q9I2Y1",47.5,8.199999999999996E-121,"pabB PA1758",{"$nulls":4},"DB01942","Formic Acid","approved, experimental","unknown"]
[100.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","Q9HVP8",52.6,8.900000000000001E-58,"coaE PA4529","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24;",null,"DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[101.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[102.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[103.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04345","7,8-dimethylalloxazine","experimental","unknown"]
[104.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[105.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[106.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[107.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[108.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","Q9HZN8",44.1,5.4E-47,"tmk PA2962",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","3UWK;3UWO;3UXM;4E5U;4EDH;4ESH;4GMD;","DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[109.0,"2.7.7.18","Nicotinate-nucleotide adenylyltransferase","Shigella flexneri","P0A753","BE0002611","Q9HX21",39.4,1.4E-39,"nadD PA4006","Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. ","FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18;","1YUL;1YUM;1YUN;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[110.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q9HT22",53.0,1.9999999999999995E-166,"glmU PA5552","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: ; Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};; CATALYTIC ACTIVITY: ; Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[111.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase 2","Shigella flexneri","P61888","BE0001912","Q9HU22",66.0,1.5999999999999997E-135,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[112.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26393","BE0001910","Q9HU22",75.2,2.799999999999999E-159,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB01861","Uridine diphosphate glucose","experimental","unknown"]
[113.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26393","BE0001910","Q9HU22",75.2,2.799999999999999E-159,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[114.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB01643","Thymidine-5'-Phosphate","experimental","unknown"]
[115.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB04485","Deoxythymidine","experimental, investigational","unknown"]
[116.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[117.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB03751","2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose","experimental","unknown"]
[118.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB03723","2'-Deoxy-Thymidine-Beta-L-Rhamnose","experimental","unknown"]
[119.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02843","alpha-D-glucose-1-phosphate","experimental","unknown"]
[120.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[121.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","Q72K87","BE0001943","Q9I6D1",53.9,7.299999999999999E-50,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03912","4'-Phosphopantetheine","experimental","unknown"]
[122.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03912","4'-Phosphopantetheine","experimental","unknown"]
[123.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03170","Dephospho Coenzyme A","experimental","unknown"]
[124.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[125.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","Q9HZM5",54.2,7.4E-86,"kdsB PA2979","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};","4XWI;","DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[126.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[127.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[128.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[129.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[130.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","Q9HVV9",40.1,4.6E-35,"PA4458",null,"FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[131.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q9HZN6",35.8,1.6E-36,"pabC PA2964",null,null,null,"2Y4R;","DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[132.0,"4.2.1.20","Tryptophan synthase alpha chain","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","P16608","BE0001719","P07344",41.1,2.7E-54,"trpA PA0035","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00131};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[133.0,"4.2.1.20","Tryptophan synthase alpha chain","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","P16608","BE0001719","P07344",41.1,2.7E-54,"trpA PA0035","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00131};",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[134.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[135.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07953","N-[1H-INDOL-3-YL-ACETYL]VALINE ACID","experimental","unknown"]
[136.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07952","N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID","experimental","unknown"]
[137.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07951","N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID","experimental","unknown"]
[138.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07925","4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[139.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07894","4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[140.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07890","4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID","experimental","unknown"]
[141.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07732","2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[142.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07748","2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[143.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07745","2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[144.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB04143","Indole-3-Glycerol Phosphate","experimental","unknown"]
[145.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07773","5-FLUOROINDOLE PROPANOL PHOSPHATE","experimental","unknown"]
[146.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB01942","Formic Acid","approved, experimental","unknown"]
[147.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB02828","5-Fluorolevulinic Acid","experimental","unknown"]
[148.0,"4.2.1.46","dTDP-glucose 4,6-dehydratase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26391","BE0001740","Q9HU24",61.0,3.5999999999999996E-154,"rmlB PA5161",null,null,"CATALYTIC ACTIVITY: Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477, ChEBI:CHEBI:57649; EC=4.2.1.46; Evidence={ECO:0000256|RuleBase:RU004473};",null,"DB03751","2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose","experimental","unknown"]
[149.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","Q9I344",43.2,1.1E-96,"aroC PA1681","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: ; Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[150.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26394","BE0001669","Q9HU21",65.7,3.899999999999999E-77,"rmlC PA5164","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000269|PubMed:17046787}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000305|PubMed:17046787};","1RTV;2IXH;2IXI;2IXJ;2IXK;","DB02549","3'-O-Acetylthymidine-5'-Diphosphate","experimental","unknown"]
[151.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU21","BE0002506","Q9HU21",100.0,1.7999999999999997E-134,"rmlC PA5164","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000269|PubMed:17046787}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000305|PubMed:17046787};","1RTV;2IXH;2IXI;2IXJ;2IXK;","DB01694","D-tartaric acid","experimental","unknown"]
[152.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Mycobacterium tuberculosis","P9WH11","BE0003322","Q9HU21",40.2,7.9E-37,"rmlC PA5164","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000269|PubMed:17046787}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000305|PubMed:17046787};","1RTV;2IXH;2IXI;2IXJ;2IXK;","DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[153.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","Q9HYQ8",53.8,2.3999999999999995E-104,"hldD rfaD PA3337","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. Bacterial outer membrane biogenesis; LPS core biosynthesis. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[154.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","Q9HYQ8",53.8,2.3999999999999995E-104,"hldD rfaD PA3337","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. Bacterial outer membrane biogenesis; LPS core biosynthesis. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[155.0,"5.3.1.1","Triosephosphate isomerase","Vibrio marinus","P50921","BE0001889","Q9HV51",50.4,7.2E-76,"tpiA PA4748","Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. ","FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.","CATALYTIC ACTIVITY: ; Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};",null,"DB02726","2-Phosphoglycolic Acid","experimental","unknown"]
[156.0,"5.3.1.24","N-(5'-phosphoribosyl)anthranilate isomerase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q56320","BE0001549","Q59649",44.8,2.0E-39,"trpF PA3113","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. ",null,"CATALYTIC ACTIVITY: ; Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24;",null,"DB03543","1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate","experimental","unknown"]
[157.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","Q9HVZ0",100.0,2.0999999999999997E-134,"gmhA PA4425","Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS core biosynthesis. ","FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate; Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203, ChEBI:CHEBI:60204; EC=5.3.1.28;","1X92;3BJZ;","DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[158.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","Q9I6G1",57.7,1.1999999999999998E-80,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[159.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","Q9I6G1",64.3,1.2999999999999998E-89,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[160.0,"5.4.99.5","Secreted chorismate mutase","Mycobacterium tuberculosis","P9WIB9","BE0004361","Q9HU05",30.3,1.6999999999999998E-12,"aroQ PA5184","Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. ","FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate. The joint presence of this enzyme together with cyclohexadienyl dehydratase and aromatic aminotransferase in the periplasmic compartment comprises a complete three-step chorismate to phenylalanine pathway and accounts for the so called hidden overflow pathway to phenylalanine in P.aeruginosa, in which two possible routes for it exists, namely either via phenylpyruvate or L-arogenate. {ECO:0000250|UniProtKB:P0A9J8, ECO:0000269|PubMed:11532214}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:11532214};",null,"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[161.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02694","Pantoyl Adenylate","experimental","unknown"]
[162.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[163.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB01930","2,4-Dihydroxy-3,3-Dimethyl-Butyrate","experimental","unknown"]
[164.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03107","Beta-Alanine","experimental","unknown"]
[165.0,"6.3.2.1","Pantothenate synthetase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","Q5SHF5","BE0004567","Q9HV69",52.6,2.7E-78,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03570","Tris-Hydroxymethyl-Methyl-Ammonium","experimental","unknown"]
[166.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[167.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[168.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[169.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[170.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[171.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[172.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[173.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[174.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[175.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[176.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[177.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[178.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[179.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[180.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[181.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[182.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[183.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[184.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[185.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[186.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[187.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[188.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[189.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[190.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]

{"sheet":"P.aeruginosa PAO1 2017 FBA-only","index":10,"n_rows":192,"n_cols":19,"rows_kept":192,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.100","3-oxoacyl-[acyl-carrier-protein] reductase FabG","Escherichia coli (strain K12)","P0AEK2","BE0002069","O54438",64.2,3.699999999999999E-101,"fabG PA2967","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;","4AFN;4AG3;4BNT;4BNU;4BNV;4BNW;4BNX;4BNY;4BNZ;4BO0;4BO1;4BO2;4BO3;4BO4;4BO5;4BO6;4BO7;4BO8;4BO9;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[1.0,"1.1.1.133","dTDP-4-dehydrorhamnose reductase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26392","BE0001971","Q9HU23",52.2,3.499999999999999E-97,"rmlD PA5162","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. ","FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. {ECO:0000256|RuleBase:RU364082}.","CATALYTIC ACTIVITY: Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378, ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62830; EC=1.1.1.133; Evidence={ECO:0000256|RuleBase:RU364082};",null,"DB03723","2'-Deoxy-Thymidine-Beta-L-Rhamnose","experimental","unknown"]
[2.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[3.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[4.0,"1.1.1.25","Shikimate dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43876","BE0001445","P43904",44.5,8.100000000000001E-61,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[5.0,"1.1.1.85","3-isopropylmalate dehydrogenase","Thiobacillus ferrooxidans","Q56268","BE0001699","Q51375",61.7,2.0999999999999996E-142,"leuB PA3118","Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. ","FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.","CATALYTIC ACTIVITY: ; Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85;",null,"DB04279","3-Isopropylmalic Acid","experimental","unknown"]
[6.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[7.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB04267","Dipicolinic Acid","experimental","unknown"]
[8.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01691","Indole Naphthyridinone","experimental","unknown"]
[9.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01865","3-(6-Aminopyridin-3-Yl)-N-Methyl-N-[(1-Methyl-1h-Indol-2-Yl)Methyl]Acrylamide","experimental","unknown"]
[10.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08605","6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[11.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08604","Triclosan","approved","unknown"]
[12.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08265","2-(TOLUENE-4-SULFONYL)-2H-BENZO[D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[13.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB02379","Beta-D-Glucose","experimental","unknown"]
[14.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03030","4-(2-Thienyl)-1-(4-Methylbenzyl)-1h-Imidazole","experimental","unknown"]
[15.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03534","3-[(Acetyl-Methyl-Amino)-Methyl]-4-Amino-N-Methyl-N-(1-Methyl-1h-Indol-2-Ylmethyl)-Benzamide","experimental","unknown"]
[16.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB04030","1,3,4,9-Tetrahydro-2-(Hydroxybenzoyl)-9-[(4-Hydroxyphenyl)Methyl]-6-Methoxy-2h-Pyrido[3,4-B]Indole","experimental","unknown"]
[17.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[18.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[19.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB04007","Bromo-WR99210","experimental","unknown"]
[20.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB00951","Isoniazid","approved","unknown"]
[21.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved","unknown"]
[22.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[23.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[24.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[25.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[26.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[27.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved","unknown"]
[28.0,"2.1.1.13","Methionine synthase","Escherichia coli (strain K12)","P13009","BE0001615","Q9I2Q2",67.7,0.0,"metH PA1843","Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. ","FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13;",null,"DB03614","Methylcobalamin","approved, experimental","unknown"]
[29.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[30.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[31.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[32.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[33.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[34.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[35.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[36.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[37.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[38.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[39.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[40.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[41.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[42.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[43.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[44.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[45.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[46.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[47.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[48.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[49.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[50.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[51.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[52.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Escherichia coli (strain K12)","P31057","BE0001744","Q9HV70",50.9,3.399999999999999E-87,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB03795","2-Dehydropantoate","experimental","unknown"]
[53.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Neisseria meningitidis serogroup B (strain MC58)","Q9JZW6","BE0001822","Q9HV70",58.4,2.9999999999999995E-95,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB04074","Alpha-ketoisovalerate","experimental","unknown"]
[54.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB02327","Triethylene glycol","experimental","unknown"]
[55.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB03361","2-{(9as)-9a-[(1s)-1-Hydroxyethyl]-2,7-Dimethyl-9a,10-Dihydro-5h-Pyrimido[4,5-D][1,3]Thiazolo[3,2-a]Pyrimidin-8-Yl}Ethyl Trihydrogen Diphosphate","experimental","unknown"]
[56.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q9HWK1",34.9,7.399999999999997E-97,"PA4180",{"$nulls":4},"DB01987","Cocarboxylase","approved, experimental","unknown"]
[57.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[58.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[59.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[60.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[61.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[62.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[63.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[64.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[65.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","Q9HW01",44.8,8.099999999999999E-90,"murG PA4412","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: ; Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};","3S2U;","DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[66.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[67.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[68.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[69.0,"2.4.2.19","Nicotinate-nucleotide pyrophosphorylase [carboxylating]","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P30012","BE0001347","P30819",57.7,1.6999999999999997E-97,"nadC PA4524","Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1. ","FUNCTION: Involved in the catabolism of quinolinic acid (QA). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate; Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017; EC=2.4.2.19;",null,"DB01796","Quinolinic Acid","experimental","unknown"]
[70.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[71.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[72.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[73.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[74.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[75.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[76.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[77.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[78.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[79.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB01819","Phosphoenolpyruvate","experimental","unknown"]
[80.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[81.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[82.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[83.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[84.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[85.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[86.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[87.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[88.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[89.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[90.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[91.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[92.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[93.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[94.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[95.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[96.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[97.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[98.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[99.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q9I2Y1",47.5,8.199999999999996E-121,"pabB PA1758",{"$nulls":4},"DB01942","Formic Acid","approved, experimental","unknown"]
[100.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","Q9HVP8",52.6,8.900000000000001E-58,"coaE PA4529","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24;",null,"DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[101.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[102.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[103.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04345","7,8-dimethylalloxazine","experimental","unknown"]
[104.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[105.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[106.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[107.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[108.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","Q9HZN8",44.1,5.4E-47,"tmk PA2962",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","3UWK;3UWO;3UXM;4E5U;4EDH;4ESH;4GMD;","DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[109.0,"2.7.7.18","Nicotinate-nucleotide adenylyltransferase","Shigella flexneri","P0A753","BE0002611","Q9HX21",39.4,1.4E-39,"nadD PA4006","Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. ","FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18;","1YUL;1YUM;1YUN;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[110.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q9HT22",53.0,1.9999999999999995E-166,"glmU PA5552","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: ; Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};; CATALYTIC ACTIVITY: ; Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[111.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase 2","Shigella flexneri","P61888","BE0001912","Q9HU22",66.0,1.5999999999999997E-135,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[112.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26393","BE0001910","Q9HU22",75.2,2.799999999999999E-159,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB01861","Uridine diphosphate glucose","experimental","unknown"]
[113.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26393","BE0001910","Q9HU22",75.2,2.799999999999999E-159,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[114.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB01643","Thymidine-5'-Phosphate","experimental","unknown"]
[115.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB04485","Deoxythymidine","experimental, investigational","unknown"]
[116.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[117.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB03751","2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose","experimental","unknown"]
[118.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB03723","2'-Deoxy-Thymidine-Beta-L-Rhamnose","experimental","unknown"]
[119.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02843","alpha-D-glucose-1-phosphate","experimental","unknown"]
[120.0,"2.7.7.24","Glucose-1-phosphate thymidylyltransferase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU22","BE0002493","Q9HU22",100.0,0.0,"rmlA PA5163",null,"FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000256|RuleBase:RU003706}.","CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477, ChEBI:CHEBI:58601; EC=2.7.7.24; Evidence={ECO:0000256|RuleBase:RU003706};","1FXO;1FZW;1G0R;1G1L;1G23;1G2V;1G3L;3ZLK;3ZLL;4ARW;4ASJ;4ASY;4B2W;4B2X;4B3U;4B42;4B4B;4B4G;4B4M;4B5B;5FTS;5FTV;5FU0;5FU8;5FUH;5FYE;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[121.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","Q72K87","BE0001943","Q9I6D1",53.9,7.299999999999999E-50,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03912","4'-Phosphopantetheine","experimental","unknown"]
[122.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03912","4'-Phosphopantetheine","experimental","unknown"]
[123.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03170","Dephospho Coenzyme A","experimental","unknown"]
[124.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[125.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","Q9HZM5",54.2,7.4E-86,"kdsB PA2979","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};","4XWI;","DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[126.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[127.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[128.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[129.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[130.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","Q9HVV9",40.1,4.6E-35,"PA4458",null,"FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[131.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q9HZN6",35.8,1.6E-36,"pabC PA2964",null,null,null,"2Y4R;","DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[132.0,"4.2.1.20","Tryptophan synthase alpha chain","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","P16608","BE0001719","P07344",41.1,2.7E-54,"trpA PA0035","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00131};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[133.0,"4.2.1.20","Tryptophan synthase alpha chain","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","P16608","BE0001719","P07344",41.1,2.7E-54,"trpA PA0035","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00131};",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[134.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[135.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07953","N-[1H-INDOL-3-YL-ACETYL]VALINE ACID","experimental","unknown"]
[136.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07952","N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID","experimental","unknown"]
[137.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07951","N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID","experimental","unknown"]
[138.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07925","4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[139.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07894","4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[140.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07890","4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID","experimental","unknown"]
[141.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07732","2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[142.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07748","2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[143.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07745","2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[144.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB04143","Indole-3-Glycerol Phosphate","experimental","unknown"]
[145.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","P07345",56.6,3.699999999999999E-151,"trpB PA0036","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;",null,"DB07773","5-FLUOROINDOLE PROPANOL PHOSPHATE","experimental","unknown"]
[146.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB01942","Formic Acid","approved, experimental","unknown"]
[147.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB02828","5-Fluorolevulinic Acid","experimental","unknown"]
[148.0,"4.2.1.46","dTDP-glucose 4,6-dehydratase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26391","BE0001740","Q9HU24",61.0,3.5999999999999996E-154,"rmlB PA5161",null,null,"CATALYTIC ACTIVITY: Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477, ChEBI:CHEBI:57649; EC=4.2.1.46; Evidence={ECO:0000256|RuleBase:RU004473};",null,"DB03751","2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose","experimental","unknown"]
[149.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","Q9I344",43.2,1.1E-96,"aroC PA1681","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: ; Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[150.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26394","BE0001669","Q9HU21",65.7,3.899999999999999E-77,"rmlC PA5164","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000269|PubMed:17046787}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000305|PubMed:17046787};","1RTV;2IXH;2IXI;2IXJ;2IXK;","DB02549","3'-O-Acetylthymidine-5'-Diphosphate","experimental","unknown"]
[151.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HU21","BE0002506","Q9HU21",100.0,1.7999999999999997E-134,"rmlC PA5164","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000269|PubMed:17046787}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000305|PubMed:17046787};","1RTV;2IXH;2IXI;2IXJ;2IXK;","DB01694","D-tartaric acid","experimental","unknown"]
[152.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Mycobacterium tuberculosis","P9WH11","BE0003322","Q9HU21",40.2,7.9E-37,"rmlC PA5164","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000269|PubMed:17046787}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000305|PubMed:17046787};","1RTV;2IXH;2IXI;2IXJ;2IXK;","DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[153.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","Q9HYQ8",53.8,2.3999999999999995E-104,"hldD rfaD PA3337","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. Bacterial outer membrane biogenesis; LPS core biosynthesis. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB01774","Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester","experimental","unknown"]
[154.0,"5.1.3.20","ADP-L-glycero-D-manno-heptose-6-epimerase","Escherichia coli (strain K12)","P67910","BE0001296","Q9HYQ8",53.8,2.3999999999999995E-104,"hldD rfaD PA3337","Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. Bacterial outer membrane biogenesis; LPS core biosynthesis. ","FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-Rule:MF_01601}.","CATALYTIC ACTIVITY: Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967, ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-Rule:MF_01601};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[155.0,"5.3.1.1","Triosephosphate isomerase","Vibrio marinus","P50921","BE0001889","Q9HV51",50.4,7.2E-76,"tpiA PA4748","Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. ","FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.","CATALYTIC ACTIVITY: ; Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};",null,"DB02726","2-Phosphoglycolic Acid","experimental","unknown"]
[156.0,"5.3.1.24","N-(5'-phosphoribosyl)anthranilate isomerase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q56320","BE0001549","Q59649",44.8,2.0E-39,"trpF PA3113","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. ",null,"CATALYTIC ACTIVITY: ; Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24;",null,"DB03543","1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate","experimental","unknown"]
[157.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","Q9HVZ0",100.0,2.0999999999999997E-134,"gmhA PA4425","Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS core biosynthesis. ","FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate; Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203, ChEBI:CHEBI:60204; EC=5.3.1.28;","1X92;3BJZ;","DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[158.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","Q9I6G1",57.7,1.1999999999999998E-80,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[159.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","Q9I6G1",64.3,1.2999999999999998E-89,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[160.0,"5.4.99.5","Secreted chorismate mutase","Mycobacterium tuberculosis","P9WIB9","BE0004361","Q9HU05",30.3,1.6999999999999998E-12,"aroQ PA5184","Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. ","FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate. The joint presence of this enzyme together with cyclohexadienyl dehydratase and aromatic aminotransferase in the periplasmic compartment comprises a complete three-step chorismate to phenylalanine pathway and accounts for the so called hidden overflow pathway to phenylalanine in P.aeruginosa, in which two possible routes for it exists, namely either via phenylpyruvate or L-arogenate. {ECO:0000250|UniProtKB:P0A9J8, ECO:0000269|PubMed:11532214}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:11532214};",null,"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[161.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02694","Pantoyl Adenylate","experimental","unknown"]
[162.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[163.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB01930","2,4-Dihydroxy-3,3-Dimethyl-Butyrate","experimental","unknown"]
[164.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03107","Beta-Alanine","experimental","unknown"]
[165.0,"6.3.2.1","Pantothenate synthetase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","Q5SHF5","BE0004567","Q9HV69",52.6,2.7E-78,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03570","Tris-Hydroxymethyl-Methyl-Ammonium","experimental","unknown"]
[166.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[167.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[168.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[169.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[170.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[171.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[172.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[173.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[174.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[175.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[176.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[177.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[178.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[179.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[180.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[181.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[182.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[183.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[184.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[185.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[186.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[187.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[188.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[189.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[190.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","P37798",71.2,0.0,"accC fabG PA4848","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;","2C00;2VQD;","DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]

{"sheet":"P.aeruginosa PAO1 2017 FBA+FVA","index":11,"n_rows":177,"n_cols":19,"rows_kept":177,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.100","3-oxoacyl-[acyl-carrier-protein] reductase FabG","Escherichia coli (strain K12)","P0AEK2","BE0002069","O54438",64.2,3.699999999999999E-101,"fabG PA2967","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;","4AFN;4AG3;4BNT;4BNU;4BNV;4BNW;4BNX;4BNY;4BNZ;4BO0;4BO1;4BO2;4BO3;4BO4;4BO5;4BO6;4BO7;4BO8;4BO9;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[1.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[2.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[3.0,"1.1.1.25","Shikimate dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43876","BE0001445","P43904",44.5,8.100000000000001E-61,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[4.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[5.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB03649","[{(5-Chloro-2-Pyridinyl)Amino} Methylene]-1,1-Bisphosphonate","experimental","unknown"]
[6.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB02948","Fosmidomycin","experimental, investigational","unknown"]
[7.0,"1.1.1.267","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Escherichia coli (strain K12)","P45568","BE0001575","Q9KGU6",57.9,8.399999999999997E-149,"dxr PA3650","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. ","FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000255|HAMAP-Rule:MF_00183};",null,"DB02496","1-Deoxy-D-xylulose 5-phosphate","experimental","unknown"]
[8.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB04267","Dipicolinic Acid","experimental","unknown"]
[9.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","P38103",63.0,3.499999999999999E-109,"dapB PA4759","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};; CATALYTIC ACTIVITY: ; Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};","4YWJ;","DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[10.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[11.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[12.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB00951","Isoniazid","approved","unknown"]
[13.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB04007","Bromo-WR99210","experimental","unknown"]
[14.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[15.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[16.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[17.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved","unknown"]
[18.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved","unknown"]
[19.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[20.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[21.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[22.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[23.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[24.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[25.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[26.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[27.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[28.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[29.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[30.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[31.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[32.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[33.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[34.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[35.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[36.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[37.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[38.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[39.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[40.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[41.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[42.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[43.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[44.0,"2.2.1.1","Transketolase 1","Escherichia coli (strain K12)","P27302","BE0003276","Q9I5Y8",73.0,0.0,"tktA PA0548",null,"FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.","CATALYTIC ACTIVITY: ; Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1; Evidence={ECO:0000256|RuleBase:RU004996};","4XEU;","DB01987","Cocarboxylase","approved, experimental","unknown"]
[45.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08359","2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE","experimental","unknown"]
[46.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB01034","Cerulenin","approved","yes","inhibitor"]
[47.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03017","Lauric Acid","approved, experimental","unknown"]
[48.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB03600","Capric acid","experimental","unknown"]
[49.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04302","4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One","experimental","unknown"]
[50.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08628","(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE","experimental","unknown"]
[51.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB08627","(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE","experimental","unknown"]
[52.0,"2.3.1.41","3-oxoacyl-[acyl-carrier-protein] synthase 1","Escherichia coli (strain K12)","P0A953","BE0000801","Q9I3B2",69.6,0.0,"fabB PA1609",{"$nulls":4},"DB04519","Caprylic acid","experimental, investigational","unknown"]
[53.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","Q9HW01",44.8,8.099999999999999E-90,"murG PA4412","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: ; Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};","3S2U;","DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[54.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[55.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[56.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[57.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[58.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[59.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02508","Isopentyl Pyrophosphate","experimental","unknown"]
[60.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB02270","Dimethylallyl S-Thiolodiphosphate","experimental","unknown"]
[61.0,"2.5.1.10","Farnesyl diphosphate synthase","Escherichia coli (strain K12)","P22939","BE0001517","Q9HWY4",52.2,6.599999999999998E-83,"ispA PA4043",null,null,null,"3ZCD;3ZL6;3ZMB;3ZMC;3ZOU;4UMJ;","DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[62.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[63.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[64.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[65.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[66.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[67.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[68.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[69.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[70.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[71.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[72.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[73.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[74.0,"2.5.1.61","Porphobilinogen deaminase","Escherichia coli (strain K12)","P06983","BE0001758","Q60169",67.8,1.0999999999999998E-138,"hemC PA5260","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. ","FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+); Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;",null,"DB04517","Dipyrromethane Cofactor","experimental","unknown"]
[75.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[76.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[77.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[78.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[79.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[80.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[81.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[82.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[83.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[84.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[85.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[86.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[87.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[88.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q9I2Y1",47.5,8.199999999999996E-121,"pabB PA1758",{"$nulls":4},"DB01942","Formic Acid","approved, experimental","unknown"]
[89.0,"2.7.1.148","4-diphosphocytidyl-2-C-methyl-D-erythritol kinase","Shigella flexneri","Q83LD8","BE0001574","P42805",54.6,2.9999999999999992E-99,"ispE PA4669","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. ","FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823, ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148; Evidence={ECO:0000255|HAMAP-Rule:MF_00061};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[90.0,"2.7.1.148","4-diphosphocytidyl-2-C-methyl-D-erythritol kinase","Shigella flexneri","Q83LD8","BE0001574","P42805",54.6,2.9999999999999992E-99,"ispE PA4669","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. ","FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823, ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148; Evidence={ECO:0000255|HAMAP-Rule:MF_00061};",null,"DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[91.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[92.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[93.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[94.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[95.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","Q9HXV4",64.4,1.6999999999999996E-91,"adk PA3686","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: ; Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[96.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q9HT22",53.0,1.9999999999999995E-166,"glmU PA5552","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: ; Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};; CATALYTIC ACTIVITY: ; Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[97.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[98.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB03854","Pentane-1,5-Diamine","experimental","unknown"]
[99.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Escherichia coli (strain K12)","Q46893","BE0001661","P57707",45.6,5.600000000000001E-53,"ispD PA3633","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: ; Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};",null,"DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[100.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[101.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[102.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[103.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[104.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB04647","BOC-GAMMA-D-GLU-L-LYS(CBZ)-D-BOROALA","experimental","unknown"]
[105.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01329","Cefoperazone","approved, investigational","yes","inhibitor"]
[106.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01331","Cefoxitin","approved","yes","inhibitor"]
[107.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli (strain K12)","P0AEB2","BE0002063","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB00274","Cefmetazole","approved, investigational","yes","inhibitor"]
[108.0,"3.4.16.4","Peptidoglycan synthase FtsI","Escherichia coli O157:H7","P0AD69","BE0003396","G3XD46",45.1,9.599999999999997E-158,"ftsI pbpB PA4418","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:20580675). {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:20580675}.","CATALYTIC ACTIVITY: ; Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-Rule:MF_02080};","3PBN;3PBO;3PBQ;3PBR;3PBS;3PBT;4KQO;4KQQ;4KQR;","DB05659","faropenem medoxomil","investigational","unknown"]
[109.0,"3.4.16.4","Peptidoglycan synthase FtsI","Escherichia coli O157:H7","P0AD69","BE0003396","Q9I1K1",41.6,3.499999999999999E-131,"pbpC PA2272","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:9045804). {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:9045804}.","CATALYTIC ACTIVITY: ; Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-Rule:MF_02080};",null,"DB05659","faropenem medoxomil","investigational","unknown"]
[110.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","P0AEB3","BE0002475","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB01147","Cloxacillin","approved, vet_approved","unknown","inhibitor"]
[111.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacA","Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","P0AEB3","BE0002475","G3XD74",47.8,1.3E-108,"dacC PA3999",{"$nulls":4},"DB04647","BOC-GAMMA-D-GLU-L-LYS(CBZ)-D-BOROALA","experimental","unknown"]
[112.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00303","Ertapenem","approved, investigational","yes","inhibitor"]
[113.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB01329","Cefoperazone","approved, investigational","yes","inhibitor"]
[114.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB01331","Cefoxitin","approved","yes","inhibitor"]
[115.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00430","Cefpiramide","approved","yes","inhibitor"]
[116.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase DacC","Escherichia coli (strain K12)","P08506","BE0003685","G3XD74",47.8,3.899999999999999E-112,"dacC PA3999",{"$nulls":4},"DB00274","Cefmetazole","approved, investigational","yes","inhibitor"]
[117.0,"3.4.16.4","D-alanyl-D-alanine carboxypeptidase","Actinomadura sp. (strain R39)","P39045","BE0003356","Q9HZG1",29.4,3.7E-32,"PA3047",{"$nulls":4},"DB04742","(2R)-2-{(1R)-2-oxo-1-[(2-thienylacetyl)amino]ethyl}-5,6-dihydro-2h-1,3-thiazine-4-carboxylic acid","experimental","unknown"]
[118.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB02129","Dihydroorotic Acid","experimental","unknown"]
[119.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB02262","Orotic Acid","experimental, investigational","unknown","inhibitor"]
[120.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[121.0,"3.5.2.3","Dihydroorotase","Escherichia coli (strain K12)","P05020","BE0001452","P72170",56.7,1.0999999999999997E-131,"pyrC PA3527","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. ","FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.","CATALYTIC ACTIVITY: ; Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219};",null,"DB04252","N-Carbamoyl-L-Aspartate","experimental","unknown"]
[122.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[123.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q59654",59.5,1.2999999999999997E-86,"pyrF PA2876","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).","CATALYTIC ACTIVITY: ; Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[124.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q9HZN6",35.8,1.6E-36,"pabC PA2964",null,null,null,"2Y4R;","DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[125.0,"4.1.3.40","Chorismate--pyruvate lyase","Escherichia coli (strain K12)","P26602","BE0001507","Q9HTK1",31.4,4.7E-13,"ubiC PA5357","Cofactor biosynthesis; ubiquinone biosynthesis. ","FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = 4-hydroxybenzoate + pyruvate; Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879, ChEBI:CHEBI:29748; EC=4.1.3.40; Evidence={ECO:0000255|HAMAP-Rule:MF_01632};",null,"DB02130","Vanillic acid","experimental","unknown"]
[126.0,"4.1.3.40","Chorismate--pyruvate lyase","Escherichia coli (strain K12)","P26602","BE0001507","Q9HTK1",31.4,4.7E-13,"ubiC PA5357","Cofactor biosynthesis; ubiquinone biosynthesis. ","FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.","CATALYTIC ACTIVITY: ; Reaction=chorismate = 4-hydroxybenzoate + pyruvate; Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879, ChEBI:CHEBI:29748; EC=4.1.3.40; Evidence={ECO:0000255|HAMAP-Rule:MF_01632};",null,"DB04242","P-Hydroxybenzoic Acid","experimental","unknown"]
[127.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB02828","5-Fluorolevulinic Acid","experimental","unknown"]
[128.0,"4.2.1.24","Delta-aminolevulinic acid dehydratase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q59643","BE0001285","Q59643",100.0,0.0,"hemB PA5243","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. ","FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:16819823};","1B4K;1GZG;1W54;1W56;1W5M;1W5N;1W5O;1W5P;1W5Q;2C13;2C14;2C15;2C16;2C18;2C19;2WOQ;","DB01942","Formic Acid","approved, experimental","unknown"]
[129.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Shigella flexneri","P0A6Q5","BE0001829","O33877",68.6,8.399999999999998E-83,"fabA PA1610","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;; CATALYTIC ACTIVITY: ; Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;; CATALYTIC ACTIVITY: ; Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;","4B0B;4B0C;4B0I;4B0J;4B8U;4CL6;4FQ9;","DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[130.0,"4.2.1.59","3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase","Escherichia coli (strain K12)","P0A6Q3","BE0004016","O33877",68.6,8.399999999999998E-83,"fabA PA1610","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;; CATALYTIC ACTIVITY: ; Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;; CATALYTIC ACTIVITY: ; Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP]; Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927, ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;","4B0B;4B0C;4B0I;4B0J;4B8U;4CL6;4FQ9;","DB03813","2-Decenoyl N-Acetyl Cysteamine","experimental","unknown"]
[131.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","Q9I344",43.2,1.1E-96,"aroC PA1681","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: ; Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[132.0,"4.3.3.7","4-hydroxy-tetrahydrodipicolinate synthase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X1K9","BE0001460","Q9I4W3",44.4,1.2999999999999997E-80,"dapA PA1010","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. ","FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). {ECO:0000305|PubMed:21396954}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00418};","3NOE;3PS7;3PUO;3QZE;3S8H;","DB02370","Nz-(1-Carboxyethyl)-Lysine","experimental","unknown"]
[133.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shewanella oneidensis (strain MR-1)","Q8EBR3","BE0004091","P57708",68.2,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB07780","FARNESYL DIPHOSPHATE","experimental","unknown"]
[134.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03687","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol","experimental","unknown"]
[135.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[136.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03961","2c-Methyl-D-Erythritol 2,4-Cyclodiphosphate","experimental","unknown"]
[137.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[138.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[139.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Shigella flexneri","P62619","BE0001303","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB01859","4-Diphosphocytidyl-2-C-Methyl-D-Erythritol 2-Phosphate","experimental","unknown"]
[140.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Escherichia coli (strain K12)","P62617","BE0004106","P57708",71.6,9.699999999999998E-71,"ispF PA3627","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000255|HAMAP-Rule:MF_00107}.","CATALYTIC ACTIVITY: ; Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00107};","5B8F;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[141.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","Q9I6G1",57.7,1.1999999999999998E-80,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[142.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","Q9I6G1",64.3,1.2999999999999998E-89,"rpiA PA0330","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: ; Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};","4X84;","DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[143.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB04522","Dexfosfoserine","experimental","unknown"]
[144.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[145.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02900","alpha-D-mannose 6-phosphate","experimental","unknown"]
[146.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02867","D-Mannose 1-Phosphate","experimental","unknown"]
[147.0,"5.4.2.2","Phosphomannomutase/phosphoglucomutase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","P26276","BE0001369","P26276",100.0,0.0,"algC PA5322","Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.","CATALYTIC ACTIVITY: ; Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};; CATALYTIC ACTIVITY: ; Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};","1K2Y;1K35;1P5D;1P5G;1PCJ;1PCM;2FKF;2FKM;2H4L;2H5A;3BKQ;3C04;3RSM;4IL8;4MRQ;","DB02843","alpha-D-glucose-1-phosphate","experimental","unknown"]
[148.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[149.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[150.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[151.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[152.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[153.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[154.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[155.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[156.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[157.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[158.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[159.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[160.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[161.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[162.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[163.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[164.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[165.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","Q9HUM6",70.9,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[166.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[167.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[168.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[169.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[170.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[171.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[172.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[173.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[174.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[175.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","Q9HXM6",70.9,0.0,"guaA PA3769","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"P.aeruginosa CCBH4851 Tier3 FBA","index":12,"n_rows":183,"n_cols":19,"rows_kept":183,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.100","3-oxoacyl-[acyl-carrier-protein] reductase FabG","Escherichia coli (strain K12)","P0AEK2","BE0002069","O54438",64.2,3.699999999999999E-101,"fabG PA2967","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;","4AFN;4AG3;4BNT;4BNU;4BNV;4BNW;4BNX;4BNY;4BNZ;4BO0;4BO1;4BO2;4BO3;4BO4;4BO5;4BO6;4BO7;4BO8;4BO9;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[1.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[2.0,"1.1.1.25","Shikimate dehydrogenase","Escherichia coli (strain K12)","P15770","BE0001927","P43904",52.9,1.9E-85,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[3.0,"1.1.1.25","Shikimate dehydrogenase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43876","BE0001445","P43904",44.5,8.100000000000001E-61,"aroE PA0025","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. ","FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[4.0,"1.14.11.21","Clavaminate synthase 1","Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602)","Q05581","BE0001314","Q9I6U7",28.7,1.2,"PA0187",{"$nulls":4},"DB01839","Propylene glycol","approved, investigational","unknown"]
[5.0,"1.14.11.21","Clavaminate synthase 1","Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602)","Q05581","BE0001314","Q9I6U7",28.7,1.2,"PA0187",{"$nulls":4},"DB01985","N-Alpha-L-Acetyl-Arginine","experimental","unknown"]
[6.0,"1.14.11.21","Clavaminate synthase 1","Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602)","Q05581","BE0001314","Q9I6U7",28.7,1.2,"PA0187",{"$nulls":4},"DB02475","Deoxyguanidinoproclavaminic acid","experimental","unknown"]
[7.0,"1.14.20.3","(5R)-carbapenem-3-carboxylate synthase","Pectobacterium carotovorum subsp. carotovorum","Q9XB59","BE0002848","Q9I6U0",22.6,0.56,"PA0194",{"$nulls":4},"DB03360","N-Acetylproline","experimental","unknown"]
[8.0,"1.14.20.3","(5R)-carbapenem-3-carboxylate synthase","Pectobacterium carotovorum subsp. carotovorum","Q9XB59","BE0002848","Q9I1G5",40.4,0.56,"PA2310",{"$nulls":4},"DB03360","N-Acetylproline","experimental","unknown"]
[9.0,"1.2.5.1","Pyruvate dehydrogenase [ubiquinone]","Escherichia coli (strain K12)","P07003","BE0000768","Q9HTQ7",44.3,2.2999999999999993E-171,"poxB PA5297",{"$nulls":4},"DB00336","Nitrofural","approved, investigational, vet_approved","yes","inhibitor"]
[10.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB02379","Beta-D-Glucose","experimental","unknown"]
[11.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01691","Indole Naphthyridinone","experimental","unknown"]
[12.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01865","3-(6-Aminopyridin-3-Yl)-N-Methyl-N-[(1-Methyl-1h-Indol-2-Yl)Methyl]Acrylamide","experimental","unknown"]
[13.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03030","4-(2-Thienyl)-1-(4-Methylbenzyl)-1h-Imidazole","experimental","unknown"]
[14.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03534","3-[(Acetyl-Methyl-Amino)-Methyl]-4-Amino-N-Methyl-N-(1-Methyl-1h-Indol-2-Ylmethyl)-Benzamide","experimental","unknown"]
[15.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB04030","1,3,4,9-Tetrahydro-2-(Hydroxybenzoyl)-9-[(4-Hydroxyphenyl)Methyl]-6-Methoxy-2h-Pyrido[3,4-B]Indole","experimental","unknown"]
[16.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08604","Triclosan","approved","unknown"]
[17.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08605","6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[18.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08265","2-(TOLUENE-4-SULFONYL)-2H-BENZO[D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[19.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[20.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q9HZM7",45.3,1.7999999999999997E-80,"murB PA2977","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: ; Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};","4JAY;4JB1;","DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[21.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[22.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[23.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved","unknown"]
[24.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[25.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[26.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[27.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved","unknown"]
[28.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB00951","Isoniazid","approved","unknown"]
[29.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB04007","Bromo-WR99210","experimental","unknown"]
[30.0,"1.8.1.4","Dihydrolipoyl dehydrogenase","Pseudomonas putida","P09063","BE0002616","Q9I1L9",72.6,0.0,"lpdV PA2250",null,"FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; Evidence={ECO:0000250|UniProtKB:P18925};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[31.0,"1.8.1.4","Dihydrolipoyl dehydrogenase","Pseudomonas fluorescens","P14218","BE0002986","Q9I3D1",99.8,0.0,"lpdG PA1587",null,"FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.; FUNCTION: Also acts in the glycine cleavage system. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4;","5U8U;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[32.0,"1.8.1.4","Dihydrolipoyl dehydrogenase","Azotobacter vinelandii","P18925","BE0002965","Q9I3D1",84.3,0.0,"lpdG PA1587",null,"FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.; FUNCTION: Also acts in the glycine cleavage system. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4;","5U8U;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[33.0,"1.8.1.9","Thioredoxin reductase","Escherichia coli (strain K12)","P0A9P4","BE0002067","Q9I592",70.8,6.199999999999998E-162,"trxB2 PA0849",null,null,"CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; Evidence={ECO:0000256|RuleBase:RU003881};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[34.0,"1.8.1.9","Thioredoxin reductase","Escherichia coli (strain K12)","P0A9P4","BE0002067","Q9I0M2",71.4,6.499999999999997E-164,"trxB1 PA2616",null,null,"CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; Evidence={ECO:0000256|RuleBase:RU003881};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[35.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[36.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[37.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[38.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[39.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[40.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[41.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[42.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[43.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[44.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[45.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[46.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[47.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[48.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[49.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[50.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[51.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[52.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[53.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[54.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[55.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[56.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[57.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[58.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Escherichia coli (strain K12)","P31057","BE0001744","Q9HV70",50.9,3.399999999999999E-87,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB03795","2-Dehydropantoate","experimental","unknown"]
[59.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Neisseria meningitidis serogroup B (strain MC58)","Q9JZW6","BE0001822","Q9HV70",58.4,2.9999999999999995E-95,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB04074","Alpha-ketoisovalerate","experimental","unknown"]
[60.0,"2.1.2.2","Phosphoribosylglycinamide formyltransferase","Escherichia coli (strain K12)","P08179","BE0001476","Q9I514",58.9,4.699999999999999E-83,"purN PA0944","Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. ","FUNCTION: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01930}.","CATALYTIC ACTIVITY: Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide; Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:58426, ChEBI:CHEBI:58457; EC=2.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01930};",null,"DB02794","N-[5'-O-Phosphono-Ribofuranosyl]-2-[2-Hydroxy-2-[4-[Glutamic Acid]-N-Carbonylphenyl]-3-[2-Amino-4-Hydroxy-Quinazolin-6-Yl]-Propanylamino]-Acetamide","experimental","unknown"]
[61.0,"2.1.2.2","Phosphoribosylglycinamide formyltransferase","Escherichia coli (strain K12)","P08179","BE0001476","Q9I514",58.9,4.699999999999999E-83,"purN PA0944","Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. ","FUNCTION: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01930}.","CATALYTIC ACTIVITY: Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide; Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:58426, ChEBI:CHEBI:58457; EC=2.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01930};",null,"DB04264","(10R)-10-Formyl-5,8,10-Trideazafolic Acid","experimental","unknown"]
[62.0,"2.1.2.2","Phosphoribosylglycinamide formyltransferase","Escherichia coli (strain K12)","P08179","BE0001476","Q9I514",58.9,4.699999999999999E-83,"purN PA0944","Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. ","FUNCTION: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01930}.","CATALYTIC ACTIVITY: Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide; Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:58426, ChEBI:CHEBI:58457; EC=2.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01930};",null,"DB02540","(10S)-10-Formyl-5,8,10-Trideazafolic Acid","experimental","unknown"]
[63.0,"2.1.2.2","Phosphoribosylglycinamide formyltransferase","Escherichia coli (strain K12)","P08179","BE0001476","Q9I514",58.9,4.699999999999999E-83,"purN PA0944","Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. ","FUNCTION: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01930}.","CATALYTIC ACTIVITY: Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide; Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:58426, ChEBI:CHEBI:58457; EC=2.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01930};",null,"DB02236","Glycinamide Ribonucleotide","experimental","unknown"]
[64.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","Q9HW01",44.8,8.099999999999999E-90,"murG PA4412","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: ; Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};","3S2U;","DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[65.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB01632","Alpha-Phosphoribosylpyrophosphoric Acid","experimental, investigational","unknown"]
[66.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","P50587",69.0,3.1999999999999994E-105,"pyrE PA5331","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: ; Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[67.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[68.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[69.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[70.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[71.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[72.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[73.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[74.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[75.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[76.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[77.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[78.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[79.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB02433","{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid","experimental","unknown"]
[80.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB03936","1-Deoxy-Ribofuranose-5'-Phosphate","experimental","unknown"]
[81.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB01819","Phosphoenolpyruvate","experimental","unknown"]
[82.0,"2.5.1.55","2-dehydro-3-deoxyphosphooctonate aldolase","Shigella flexneri","P0A716","BE0001394","Q9ZFK4",68.9,4.699999999999999E-139,"kdsA PA3636","Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ",null,"CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;","4LU0;","DB03113","3-Fluoro-2-(Phosphonooxy)Propanoic Acid","experimental","unknown"]
[83.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[84.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[85.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[86.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[87.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[88.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[89.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[90.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[91.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[92.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[93.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[94.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[95.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[96.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[97.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[98.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[99.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q9I2Y1",47.5,8.199999999999996E-121,"pabB PA1758",{"$nulls":4},"DB01942","Formic Acid","approved, experimental","unknown"]
[100.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","Q9HVP8",52.6,8.900000000000001E-58,"coaE PA4529","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24;",null,"DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[101.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04345","7,8-dimethylalloxazine","experimental","unknown"]
[102.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[103.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[104.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[105.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[106.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[107.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q9HZ70",60.4,1.3999999999999998E-87,"cmk PA3163",null,null,"CATALYTIC ACTIVITY: ; Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};; CATALYTIC ACTIVITY: ; Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[108.0,"2.7.4.9","Thymidylate kinase","Shigella flexneri","P0A721","BE0001932","Q9HZN8",44.1,5.4E-47,"tmk PA2962",null,"FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","3UWK;3UWO;3UXM;4E5U;4EDH;4ESH;4GMD;","DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[109.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB02119","6-Hydroxymethyl-7,8-Dihydropterin","experimental","unknown"]
[110.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[111.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB04610","7,8-dihydro-6-hydroxymethyl-7-methyl-7-[2-phenylethyl]-pterin","experimental","unknown"]
[112.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB03197","6-Hydroxymethylpterin","experimental","unknown"]
[113.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB04047","[Pterin-6-Yl Methanyl]-Phosphonophosphate","experimental","unknown"]
[114.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB04158","6-(Adenosine Tetraphosphate-Methyl)-7,8-Dihydropterin","experimental","unknown"]
[115.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43777","BE0001488","Q9HV71",55.9,1.8E-46,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB02278","7,8-Dihydro-7,7-Dimethyl-6-Hydroxypterin","experimental","unknown"]
[116.0,"2.7.7.18","Nicotinate-nucleotide adenylyltransferase","Shigella flexneri","P0A753","BE0002611","Q9HX21",39.4,1.4E-39,"nadD PA4006","Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. ","FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18;","1YUL;1YUM;1YUN;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[117.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03912","4'-Phosphopantetheine","experimental","unknown"]
[118.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[119.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03170","Dephospho Coenzyme A","experimental","unknown"]
[120.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","Q72K87","BE0001943","Q9I6D1",53.9,7.299999999999999E-50,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03912","4'-Phosphopantetheine","experimental","unknown"]
[121.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","Q9HZM5",54.2,7.4E-86,"kdsB PA2979","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};","4XWI;","DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[122.0,"2.8.1.6","Biotin synthase","Escherichia coli (strain K12)","P12996","BE0001731","Q9I618",69.9,1.2999999999999996E-171,"bioB PA0500","Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. ","FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. {ECO:0000255|HAMAP-Rule:MF_01694}.","CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-SH + dethiobiotin + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:17319, ChEBI:CHEBI:29917, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57586, ChEBI:CHEBI:57844, ChEBI:CHEBI:57861, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428; EC=2.8.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01694};",null,"DB03775","D-Dethiobiotin","experimental","unknown"]
[123.0,"2.8.1.6","Biotin synthase","Escherichia coli (strain K12)","P12996","BE0001731","Q9I618",69.9,1.2999999999999996E-171,"bioB PA0500","Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. ","FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. {ECO:0000255|HAMAP-Rule:MF_01694}.","CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-SH + dethiobiotin + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:17319, ChEBI:CHEBI:29917, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57586, ChEBI:CHEBI:57844, ChEBI:CHEBI:57861, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428; EC=2.8.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01694};",null,"DB03754","Tromethamine","approved","unknown"]
[124.0,"3.1.1.1","Carboxylesterase 2","Pseudomonas fluorescens","Q53547","BE0003048","Q9HXE7",64.1,1.4E-89,"PA3859",null,null,null,"3CN7;3CN9;","DB03297","Benzylsulfinic Acid","experimental","unknown"]
[125.0,"3.1.1.1","Esterase EstA","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","O33407","BE0003982","Q9I6G3",25.6,7.400000000000001E-6,"PA0328",{"$nulls":4},"DB04233","(Hydroxyethyloxy)Tri(Ethyloxy)Octane","experimental","unknown"]
[126.0,"3.1.1.1","Esterase EstA","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","O33407","BE0003982","O33407",100.0,0.0,"estA papA PA5112",null,"FUNCTION: Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation; the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta-naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible. {ECO:0000269|PubMed:17631636, ECO:0000269|PubMed:20931591}.","CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:20931591};","3KVN;","DB04233","(Hydroxyethyloxy)Tri(Ethyloxy)Octane","experimental","unknown"]
[127.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[128.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[129.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[130.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[131.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","Q9HVV9",40.1,4.6E-35,"PA4458",null,"FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[132.0,"3.5.1.5","Urease","Helicobacter pylori","Q8KT33","BE0008660","Q9HUU5",66.1,1.3999999999999997E-177,"ureC PA4868","Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01953};",null,"DB09513","Urea C-14","approved","yes","substrate"]
[133.0,"3.5.1.5","Urease","Helicobacter pylori","Q8KT33","BE0008660","Q9HUU5",66.1,1.3999999999999997E-177,"ureC PA4868","Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01953};",null,"DB09510","Urea C-13","approved","yes","substrate"]
[134.0,"3.5.1.5","Urease subunit alpha","Enterobacter aerogenes","P18314","BE0000334","Q9HUU5",75.7,0.0,"ureC PA4868","Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01953};",null,"DB05265","Ecabet","approved, investigational","yes","inhibitor"]
[135.0,"3.5.1.5","Urease subunit alpha","Enterobacter aerogenes","P18314","BE0000334","Q9HUU5",75.7,0.0,"ureC PA4868","Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01953};",null,"DB00551","Acetohydroxamic Acid","approved","yes","inhibitor"]
[136.0,"3.5.1.5","Urease subunit beta","Bacillus pasteurii","P41021","BE0004009","Q9HUU6",56.4,7.299999999999999E-34,"ureB PA4867","Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01954};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[137.0,"3.5.3.23","N-succinylarginine dihydrolase","Escherichia coli (strain K12)","P76216","BE0001871","O50175",59.2,9.399999999999998E-176,"astB aruB PA0899","Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 2/5. ","FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).","CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 H2O + N(2)-succinyl-L-arginine = CO2 + N(2)-succinyl-L-ornithine + 2 NH4(+); Xref=Rhea:RHEA:19533, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938, ChEBI:CHEBI:58241, ChEBI:CHEBI:58514; EC=3.5.3.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01172};",null,"DB02501","N~2~-Succinylarginine","experimental","unknown"]
[138.0,"3.5.3.23","N-succinylarginine dihydrolase","Escherichia coli (strain K12)","P76216","BE0001871","O50175",59.2,9.399999999999998E-176,"astB aruB PA0899","Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 2/5. ","FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).","CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 H2O + N(2)-succinyl-L-arginine = CO2 + N(2)-succinyl-L-ornithine + 2 NH4(+); Xref=Rhea:RHEA:19533, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938, ChEBI:CHEBI:58241, ChEBI:CHEBI:58514; EC=3.5.3.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01172};",null,"DB03582","N~2~-Succinylornithine","experimental","unknown"]
[139.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q9HWZ6",62.9,1.3E-74,"ppa PA4031",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};","4XEL;","DB06851","N-(pyridin-3-ylmethyl)aniline","experimental","unknown"]
[140.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q9HWZ6",62.9,1.3E-74,"ppa PA4031",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};","4XEL;","DB07291","5-amino-1-(4-chlorophenyl)-1H-pyrazole-4-carbonitrile","experimental","unknown"]
[141.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Escherichia coli (strain K12)","P06968","BE0001364","Q9HTN3",71.1,2.4999999999999993E-72,"dut PA5321","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00116};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[142.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Escherichia coli (strain K12)","P06968","BE0001364","Q9HTN3",71.1,2.4999999999999993E-72,"dut PA5321","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00116};",null,"DB03413","Deoxyuridine-5'-Diphosphate","experimental","unknown"]
[143.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Escherichia coli (strain K12)","P06968","BE0001364","Q9HTN3",71.1,2.4999999999999993E-72,"dut PA5321","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00116};",null,"DB02333","Deoxyuridine-5'-Triphosphate","experimental","unknown"]
[144.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Escherichia coli (strain K12)","P06968","BE0001364","Q9HTN3",71.1,2.4999999999999993E-72,"dut PA5321","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00116};",null,"DB01965","2'-Deoxyuridine 5'-Alpha,Beta-Imido-Triphosphate","experimental","unknown"]
[145.0,"3.6.1.55","8-oxo-dGTP diphosphatase","Escherichia coli (strain K12)","P08337","BE0001520","Q9HW06",37.4,1.8000000000000001E-22,"PA4400",{"$nulls":4},"DB02023","8-Oxo-2'-Deoxy-Guanosine-5'-Monophosphate","experimental","unknown"]
[146.0,"4.1.1.31","Phosphoenolpyruvate carboxylase","Escherichia coli (strain K12)","P00864","BE0001837","Q9HXV3",55.9,0.0,"ppc PA3687",null,"FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-Rule:MF_00595}.","CATALYTIC ACTIVITY: Reaction=oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31; Evidence={ECO:0000255|HAMAP-Rule:MF_00595};",null,"DB04317","3,3-Dichloro-2-Phosphonomethyl-Acrylic Acid","experimental","unknown"]
[147.0,"4.2.1.46","dTDP-glucose 4,6-dehydratase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26391","BE0001740","Q9HU24",61.0,3.5999999999999996E-154,"rmlB PA5161",null,null,"CATALYTIC ACTIVITY: Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477, ChEBI:CHEBI:57649; EC=4.2.1.46; Evidence={ECO:0000256|RuleBase:RU004473};",null,"DB03751","2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose","experimental","unknown"]
[148.0,"4.3.3.7","4-hydroxy-tetrahydrodipicolinate synthase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X1K9","BE0001460","Q9I4W3",44.4,1.2999999999999997E-80,"dapA PA1010","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. ","FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). {ECO:0000305|PubMed:21396954}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00418};","3NOE;3PS7;3PUO;3QZE;3S8H;","DB02370","Nz-(1-Carboxyethyl)-Lysine","experimental","unknown"]
[149.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03107","Beta-Alanine","experimental","unknown"]
[150.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02694","Pantoyl Adenylate","experimental","unknown"]
[151.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[152.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB01930","2,4-Dihydroxy-3,3-Dimethyl-Butyrate","experimental","unknown"]
[153.0,"6.3.2.1","Pantothenate synthetase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","Q5SHF5","BE0004567","Q9HV69",52.6,2.7E-78,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03570","Tris-Hydroxymethyl-Methyl-Ammonium","experimental","unknown"]
[154.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[155.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[156.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[157.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[158.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[159.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[160.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[161.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[162.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[163.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[164.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[165.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[166.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[167.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[168.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[169.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[170.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[171.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","Q9HUM6",70.9,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[172.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[173.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[174.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[175.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[176.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[177.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[178.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[179.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[180.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[181.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","Q9HXM6",70.9,0.0,"guaA PA3769","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"Página6","index":13,"n_rows":140,"n_cols":19,"rows_kept":140,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.100","3-oxoacyl-[acyl-carrier-protein] reductase FabG","Escherichia coli (strain K12)","P0AEK2","BE0002069","O54438",64.2,3.699999999999999E-101,"fabG PA2967","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;","4AFN;4AG3;4BNT;4BNU;4BNV;4BNW;4BNX;4BNY;4BNZ;4BO0;4BO1;4BO2;4BO3;4BO4;4BO5;4BO6;4BO7;4BO8;4BO9;","DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[1.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03030","4-(2-Thienyl)-1-(4-Methylbenzyl)-1h-Imidazole","experimental","unknown"]
[2.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB03534","3-[(Acetyl-Methyl-Amino)-Methyl]-4-Amino-N-Methyl-N-(1-Methyl-1h-Indol-2-Ylmethyl)-Benzamide","experimental","unknown"]
[3.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB04030","1,3,4,9-Tetrahydro-2-(Hydroxybenzoyl)-9-[(4-Hydroxyphenyl)Methyl]-6-Methoxy-2h-Pyrido[3,4-B]Indole","experimental","unknown"]
[4.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB02379","Beta-D-Glucose","experimental","unknown"]
[5.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08265","2-(TOLUENE-4-SULFONYL)-2H-BENZO[D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[6.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08604","Triclosan","approved","unknown"]
[7.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB08605","6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL","experimental","unknown"]
[8.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01691","Indole Naphthyridinone","experimental","unknown"]
[9.0,"1.3.1.9","Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","Escherichia coli (strain K12)","P0AEK4","BE0002006","Q9ZFE4",69.2,2.2E-123,"fabI PA1806","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;","4NQZ;4NR0;","DB01865","3-(6-Aminopyridin-3-Yl)-N-Methyl-N-[(1-Methyl-1h-Indol-2-Yl)Methyl]Acrylamide","experimental","unknown"]
[10.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB04007","Bromo-WR99210","experimental","unknown"]
[11.0,"1.5.1.3","Dihydrofolate reductase","Mycobacterium tuberculosis","P9WNX1","BE0001944","Q9I6E3",45.9,2.9999999999999996E-28,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB00951","Isoniazid","approved","unknown"]
[12.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[13.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[14.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved","unknown"]
[15.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[16.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved","unknown"]
[17.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[18.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q9I6E3",44.8,1.3E-39,"folA PA0350","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: ; Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[19.0,"1.8.1.4","Dihydrolipoyl dehydrogenase","Pseudomonas fluorescens","P14218","BE0002986","Q9I3D1",99.8,0.0,"lpdG PA1587",null,"FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.; FUNCTION: Also acts in the glycine cleavage system. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4;","5U8U;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[20.0,"1.8.1.4","Dihydrolipoyl dehydrogenase","Azotobacter vinelandii","P18925","BE0002965","Q9I3D1",84.3,0.0,"lpdG PA1587",null,"FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.; FUNCTION: Also acts in the glycine cleavage system. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4;","5U8U;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[21.0,"1.8.1.4","Dihydrolipoyl dehydrogenase","Pseudomonas putida","P09063","BE0002616","Q9I1L9",72.6,0.0,"lpdV PA2250",null,"FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; Evidence={ECO:0000250|UniProtKB:P18925};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[22.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04503","Sp-722","experimental","unknown"]
[23.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[24.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04696","4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN","experimental","unknown"]
[25.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB08131","2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID","experimental","unknown"]
[26.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04457","2'-Deoxyguanosine-5'-Monophosphate","experimental","unknown"]
[27.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04586","2-bromophenol","experimental","unknown"]
[28.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB04447","1,4-Dithiothreitol","experimental","unknown"]
[29.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03558","Sp-876","experimental","unknown"]
[30.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[31.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03818","N-[Tosyl-D-Prolinyl]Amino-Ethanethiol","experimental","unknown"]
[32.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02256","2'-Deoxyuridine","experimental","unknown"]
[33.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[34.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02467","L-methionine (S)-S-oxide","experimental","unknown"]
[35.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02752","Tosyl-D-Proline","experimental","unknown"]
[36.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02031","(6S)-5,6,7,8-tetrahydrofolate","experimental","unknown"]
[37.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02899","N-Carboxymethionine","experimental","unknown"]
[38.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03157","N,O-Didansyl-L-Tyrosine","experimental","unknown"]
[39.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03274","2'-5'dideoxyuridine","experimental","unknown"]
[40.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03541","10-Propargyl-5,8-Dideazafolic Acid","experimental","unknown"]
[41.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[42.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03038","LY341770","experimental","unknown"]
[43.0,"2.1.1.45","Thymidylate synthase","Escherichia coli (strain K12)","P0A884","BE0001438","Q9I6F1",69.7,7.399999999999998E-143,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB02223","Ly231514 Tetra Glu","experimental","unknown"]
[44.0,"2.1.1.45","Thymidylate synthase 1","Bacillus subtilis (strain 168)","P0CI79","BE0004794","Q9I6F1",39.6,8.6E-60,"thyA PA0342","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.","CATALYTIC ACTIVITY: ; Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008};",null,"DB03761","5-Fluoro-2'-Deoxyuridine-5'-Monophosphate","experimental","unknown"]
[45.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Escherichia coli (strain K12)","P31057","BE0001744","Q9HV70",50.9,3.399999999999999E-87,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB03795","2-Dehydropantoate","experimental","unknown"]
[46.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Neisseria meningitidis serogroup B (strain MC58)","Q9JZW6","BE0001822","Q9HV70",58.4,2.9999999999999995E-95,"panB2 PA4729","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB04074","Alpha-ketoisovalerate","experimental","unknown"]
[47.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","Q9HW01",44.8,8.099999999999999E-90,"murG PA4412","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-Rule:MF_00033}.","CATALYTIC ACTIVITY: ; Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};","3S2U;","DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[48.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[49.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[50.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q51342",64.8,0.0,"purF PA3108","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: ; Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-Rule:MF_01931};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[51.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01581","Sulfamerazine","approved, vet_approved","yes","inhibitor"]
[52.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01582","Sulfamethazine","approved, investigational, vet_approved","yes","inhibitor"]
[53.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB06729","Sulfaphenazole","approved","yes","inhibitor"]
[54.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00259","Sulfanilamide","approved","yes","inhibitor"]
[55.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00634","Sulfacetamide","approved","yes","inhibitor"]
[56.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00263","Sulfisoxazole","approved, vet_approved","yes","inhibitor"]
[57.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB00576","Sulfamethizole","approved, investigational, vet_approved","yes","inhibitor"]
[58.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01015","Sulfamethoxazole","approved","yes","inhibitor"]
[59.0,"2.5.1.15","Dihydropteroate synthase","Escherichia coli (strain K12)","P0AC13","BE0000803","Q9HV49",61.1,1.4999999999999995E-104,"folP PA4750","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. ","FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000256|RuleBase:RU361205}.",null,null,"DB01298","Sulfacytine","approved","yes","inhibitor"]
[60.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[61.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[62.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q9I5Z0",72.9,0.0,"metK PA0546","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[63.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[64.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[65.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[66.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[67.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q9HVW7",61.3,2.999999999999999E-175,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[68.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q9HVW7",60.1,7.999999999999997E-173,"murA PA4450","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: ; Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","5BQ2;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[69.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[70.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[71.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[72.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine Hydroxamate","experimental","unknown"]
[73.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[74.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q9HT25",62.7,0.0,"glmS PA5549",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: ; Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[75.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q9I2Y1",47.5,8.199999999999996E-121,"pabB PA1758",{"$nulls":4},"DB01942","Formic Acid","approved, experimental","unknown"]
[76.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","Q9HVP8",52.6,8.900000000000001E-58,"coaE PA4529","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24;",null,"DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[77.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04345","7,8-dimethylalloxazine","experimental","unknown"]
[78.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[79.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q9HVM3",38.8,5.0E-43,"ribF PA4561","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB03247","Riboflavin Monophosphate","approved","unknown"]
[80.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB02119","6-Hydroxymethyl-7,8-Dihydropterin","experimental","unknown"]
[81.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB03197","6-Hydroxymethylpterin","experimental","unknown"]
[82.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB04047","[Pterin-6-Yl Methanyl]-Phosphonophosphate","experimental","unknown"]
[83.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB04158","6-(Adenosine Tetraphosphate-Methyl)-7,8-Dihydropterin","experimental","unknown"]
[84.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB04610","7,8-dihydro-6-hydroxymethyl-7-methyl-7-[2-phenylethyl]-pterin","experimental","unknown"]
[85.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Escherichia coli (strain K12)","P26281","BE0001450","Q9HV71",51.3,6.3E-49,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[86.0,"2.7.6.3","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43777","BE0001488","Q9HV71",55.9,1.8E-46,"folK PA4728","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. ",null,"CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;",null,"DB02278","7,8-Dihydro-7,7-Dimethyl-6-Hydroxypterin","experimental","unknown"]
[87.0,"2.7.7.18","Nicotinate-nucleotide adenylyltransferase","Shigella flexneri","P0A753","BE0002611","Q9HX21",39.4,1.4E-39,"nadD PA4006","Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. ","FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18;","1YUL;1YUM;1YUN;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[88.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[89.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03170","Dephospho Coenzyme A","experimental","unknown"]
[90.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q9I6D1",61.6,9.899999999999999E-62,"coaD PA0363","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};","5X6F;","DB03912","4'-Phosphopantetheine","experimental","unknown"]
[91.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","Q9HZM5",54.2,7.4E-86,"kdsB PA2979","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};","4XWI;","DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[92.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB02823","Phosphonoacetic Acid","experimental","unknown"]
[93.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB03498","Mercaptomethyl Phosphonate","experimental","unknown"]
[94.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04031","Serine Vanadate","experimental","unknown"]
[95.0,"3.1.3.1","Alkaline phosphatase","Escherichia coli (strain K12)","P00634","BE0001896","P35483",73.9,0.0,"phoA PA3296",null,"FUNCTION: Has only phosphomonoesterase activity. {ECO:0000269|PubMed:8454193}.","CATALYTIC ACTIVITY: ; Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};",null,"DB04522","Dexfosfoserine","experimental","unknown"]
[96.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","Q9HVV9",40.1,4.6E-35,"PA4458",null,"FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[97.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q9HWZ6",62.9,1.3E-74,"ppa PA4031",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};","4XEL;","DB07291","5-amino-1-(4-chlorophenyl)-1H-pyrazole-4-carbonitrile","experimental","unknown"]
[98.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q9HWZ6",62.9,1.3E-74,"ppa PA4031",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};","4XEL;","DB06851","N-(pyridin-3-ylmethyl)aniline","experimental","unknown"]
[99.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Escherichia coli (strain K12)","P06968","BE0001364","Q9HTN3",71.1,2.4999999999999993E-72,"dut PA5321","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00116};",null,"DB01965","2'-Deoxyuridine 5'-Alpha,Beta-Imido-Triphosphate","experimental","unknown"]
[100.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Escherichia coli (strain K12)","P06968","BE0001364","Q9HTN3",71.1,2.4999999999999993E-72,"dut PA5321","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00116};",null,"DB03800","2'-deoxyuridylic acid","experimental","unknown"]
[101.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Escherichia coli (strain K12)","P06968","BE0001364","Q9HTN3",71.1,2.4999999999999993E-72,"dut PA5321","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00116};",null,"DB02333","Deoxyuridine-5'-Triphosphate","experimental","unknown"]
[102.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Escherichia coli (strain K12)","P06968","BE0001364","Q9HTN3",71.1,2.4999999999999993E-72,"dut PA5321","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00116};",null,"DB03413","Deoxyuridine-5'-Diphosphate","experimental","unknown"]
[103.0,"3.6.1.55","8-oxo-dGTP diphosphatase","Escherichia coli (strain K12)","P08337","BE0001520","Q9HW06",37.4,1.8000000000000001E-22,"PA4400",{"$nulls":4},"DB02023","8-Oxo-2'-Deoxy-Guanosine-5'-Monophosphate","experimental","unknown"]
[104.0,"4.2.1.46","dTDP-glucose 4,6-dehydratase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P26391","BE0001740","Q9HU24",61.0,3.5999999999999996E-154,"rmlB PA5161",null,null,"CATALYTIC ACTIVITY: Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477, ChEBI:CHEBI:57649; EC=4.2.1.46; Evidence={ECO:0000256|RuleBase:RU004473};",null,"DB03751","2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose","experimental","unknown"]
[105.0,"4.3.3.7","4-hydroxy-tetrahydrodipicolinate synthase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X1K9","BE0001460","Q9I4W3",44.4,1.2999999999999997E-80,"dapA PA1010","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. ","FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). {ECO:0000305|PubMed:21396954}.","CATALYTIC ACTIVITY: ; Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00418};","3NOE;3PS7;3PUO;3QZE;3S8H;","DB02370","Nz-(1-Carboxyethyl)-Lysine","experimental","unknown"]
[106.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[107.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB01930","2,4-Dihydroxy-3,3-Dimethyl-Butyrate","experimental","unknown"]
[108.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03107","Beta-Alanine","experimental","unknown"]
[109.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","Q9HV69",50.7,2.3999999999999996E-69,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB02694","Pantoyl Adenylate","experimental","unknown"]
[110.0,"6.3.2.1","Pantothenate synthetase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","Q5SHF5","BE0004567","Q9HV69",52.6,2.7E-78,"panC PA4730","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03570","Tris-Hydroxymethyl-Methyl-Ammonium","experimental","unknown"]
[111.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[112.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[113.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q59650",49.4,1.0999999999999998E-132,"murE PA4417","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: ; Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[114.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[115.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[116.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q9HW02",56.8,0.0,"murC PA4411","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: ; Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};","5VVW;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[117.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[118.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[119.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[120.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[121.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[122.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[123.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[124.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q9HVZ9",51.1,1.3999999999999996E-124,"murD PA4414","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).","CATALYTIC ACTIVITY: ; Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[125.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[126.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[127.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[128.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[129.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[130.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[131.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[132.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[133.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q9HUM6",70.2,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[134.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","Q9HUM6",70.9,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane","experimental","unknown"]
[135.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[136.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[137.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q9HUM6",70.0,0.0,"purA PA4938","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: ; Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[138.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","Q9HXM6",70.9,0.0,"guaA PA3769","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.","CATALYTIC ACTIVITY: ; Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"M. tuberculosis FBA+FVA","index":14,"n_rows":125,"n_cols":19,"rows_kept":125,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.17.4.1","Ribonucleoside-diphosphate reductase 2 subunit alpha","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","Q08698","BE0001782","P9WH75",72.9,0.0,"nrdE Rv3051c MTV012.66c","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. When coexpressed in E.coli with nrdF2 the 2 proteins complement a temperature-sensitive E.coli mutant, however coexpression with nrdF1 does not complement. {ECO:0000269|PubMed:9335290}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000269|PubMed:9335290};",null,"DB03258","2'-Deoxycytidine 5'-triphosphate","experimental","unknown"]
[1.0,"1.17.4.1","Ribonucleoside-diphosphate reductase 2 subunit alpha","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","Q08698","BE0001782","P9WH75",72.9,0.0,"nrdE Rv3051c MTV012.66c","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. When coexpressed in E.coli with nrdF2 the 2 proteins complement a temperature-sensitive E.coli mutant, however coexpression with nrdF1 does not complement. {ECO:0000269|PubMed:9335290}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000269|PubMed:9335290};",null,"DB03222","dATP","experimental","unknown"]
[2.0,"1.17.4.1","Ribonucleoside-diphosphate reductase 2 subunit alpha","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","Q08698","BE0001782","P9WH75",72.9,0.0,"nrdE Rv3051c MTV012.66c","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. When coexpressed in E.coli with nrdF2 the 2 proteins complement a temperature-sensitive E.coli mutant, however coexpression with nrdF1 does not complement. {ECO:0000269|PubMed:9335290}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000269|PubMed:9335290};",null,"DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[3.0,"1.17.4.1","Ribonucleoside-diphosphate reductase subunit beta","Mycobacterium leprae (strain TN)","Q9CBQ2","BE0003267","P9WH73",71.2,1.5999999999999994E-166,"nrdF1 Rv1981c MTCY39.38","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity). Two genes for this protein are present in M.tuberculosis; this is thought to not be the active form. When coexpressed in E.coli with nrdE the 2 proteins do not complement a temperature-sensitive E.coli mutant, whereas the other gene (nrdF2) does complement. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10014};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[4.0,"1.17.4.1","Ribonucleoside-diphosphate reductase subunit beta","Mycobacterium leprae (strain TN)","Q9CBQ2","BE0003267","P9WH71",93.5,0.0,"nrdF2 Rv3048c","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Two genes for this protein are present in M.tuberculosis; this is the active form. When coexpressed in E.coli with nrdE the 2 proteins complement a temperature-sensitive E.coli mutant. {ECO:0000269|PubMed:9335290}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10014, ECO:0000269|PubMed:9335290};","1UZR;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[5.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q79FX8",50.0,1.1999999999999999E-95,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[6.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q79FX8",50.0,1.1999999999999999E-95,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[7.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB1",51.5,1.1999999999999997E-96,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[8.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB1",51.5,1.1999999999999997E-96,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[9.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P0CH91",51.9,7.699999999999997E-102,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[10.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P0CH91",51.9,7.699999999999997E-102,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[11.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q6MX39",53.4,5.299999999999999E-103,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[12.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q6MX39",53.4,5.299999999999999E-103,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[13.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB7",55.7,3.5999999999999996E-106,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[14.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB7",55.7,3.5999999999999996E-106,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[15.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q79FX6",55.9,8.1E-110,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[16.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q79FX6",55.9,8.1E-110,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[17.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB3",58.4,1.9999999999999994E-115,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[18.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB3",58.4,1.9999999999999994E-115,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[19.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB5",100.0,0.0,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[20.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB5",100.0,0.0,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[21.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB1",53.4,1.6999999999999995E-102,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[22.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB1",53.4,1.6999999999999995E-102,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[23.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q6MX39",55.2,4.899999999999999E-107,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[24.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q6MX39",55.2,4.899999999999999E-107,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[25.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB5",55.9,7.699999999999997E-110,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01718","Cetrimonium","approved","unknown"]
[26.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB5",55.9,7.699999999999997E-110,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[27.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q79FX8",57.0,7.499999999999997E-110,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01718","Cetrimonium","approved","unknown"]
[28.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q79FX8",57.0,7.499999999999997E-110,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[29.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P0CH91",69.1,1.9999999999999995E-141,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[30.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P0CH91",69.1,1.9999999999999995E-141,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[31.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB7",73.5,2.1999999999999995E-155,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01718","Cetrimonium","approved","unknown"]
[32.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB7",73.5,2.1999999999999995E-155,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[33.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q79FX6",100.0,0.0,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01718","Cetrimonium","approved","unknown"]
[34.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q79FX6",100.0,0.0,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[35.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB3",73.1,4.299999999999998E-146,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01718","Cetrimonium","approved","unknown"]
[36.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB3",73.1,4.299999999999998E-146,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[37.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","Q79FX8",55.6,7.599999999999998E-105,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[38.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P9WPB1",54.6,4.599999999999999E-105,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[39.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","Q6MX39",57.4,6.399999999999998E-110,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[40.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P9WPB5",58.4,1.8999999999999997E-115,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[41.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P0CH91",64.3,5.799999999999998E-129,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[42.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P9WPB3",100.0,0.0,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[43.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P9WPB7",72.8,9.599999999999997E-150,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[44.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","Q79FX6",73.1,4.299999999999998E-146,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[45.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P9WPB7",100.0,0.0,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01718","Cetrimonium","approved","unknown"]
[46.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","Q6MX39",56.7,6.399999999999998E-110,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[47.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","Q79FX6",73.5,2.1999999999999995E-155,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01718","Cetrimonium","approved","unknown"]
[48.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P9WPB3",72.8,9.599999999999997E-150,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01718","Cetrimonium","approved","unknown"]
[49.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P0CH91",68.6,3.7999999999999986E-139,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[50.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P9WPB1",57.0,4.4999999999999995E-110,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[51.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P9WPB5",55.7,3.4E-106,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01718","Cetrimonium","approved","unknown"]
[52.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","Q79FX8",58.7,8.999999999999999E-116,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01718","Cetrimonium","approved","unknown"]
[53.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQP3",67.3,1.4999999999999994E-165,"fbpA mpt44 Rv3804c MTV026.09c",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan, and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA. {ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:21819455, ECO:0000269|PubMed:3141278, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:21819455}; CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; Evidence={ECO:0000269|PubMed:21819455};","1SFR;","DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[54.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQP3",67.3,1.4999999999999994E-165,"fbpA mpt44 Rv3804c MTV026.09c",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan, and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA. {ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:21819455, ECO:0000269|PubMed:3141278, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:21819455}; CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; Evidence={ECO:0000269|PubMed:21819455};","1SFR;","DB02811","Diethylphosphono Group","experimental","unknown"]
[55.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQP1",71.6,7.199999999999997E-163,"fbpB Rv1886c MTCY180.32",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. {ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:3141278, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;","1F0N;1F0P;5TRZ;5TS1;","DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[56.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQP1",71.6,7.199999999999997E-163,"fbpB Rv1886c MTCY180.32",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. {ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:3141278, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;","1F0N;1F0P;5TRZ;5TS1;","DB02811","Diethylphosphono Group","experimental","unknown"]
[57.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQN7",40.5,8.199999999999998E-65,"mpt51 fbpC1 fbpD mpb51 Rv3803c MTV026.08c",null,"FUNCTION: May have a role in host tissue attachment, whereby ligands may include the serum protein fibronectin and small sugars. {ECO:0000269|PubMed:14672660}.",null,"1R88;","DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[58.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQN7",40.5,8.199999999999998E-65,"mpt51 fbpC1 fbpD mpb51 Rv3803c MTV026.08c",null,"FUNCTION: May have a role in host tissue attachment, whereby ligands may include the serum protein fibronectin and small sugars. {ECO:0000269|PubMed:14672660}.",null,"1R88;","DB02811","Diethylphosphono Group","experimental","unknown"]
[59.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQN9",100.0,0.0,"fbpC mpt45 Rv0129c MTCI5.03c",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria to fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. {ECO:0000269|PubMed:1830294, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122;","1DQY;1DQZ;1VA5;3HRH;4MQL;4MQM;4QDO;4QDT;4QDU;4QDX;4QDZ;4QE3;4QEK;5KWI;5KWJ;5OCJ;","DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[60.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQN9",100.0,0.0,"fbpC mpt45 Rv0129c MTCI5.03c",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria to fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. {ECO:0000269|PubMed:1830294, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122;","1DQY;1DQZ;1VA5;3HRH;4MQL;4MQM;4QDO;4QDT;4QDU;4QDX;4QDZ;4QE3;4QEK;5KWI;5KWJ;5OCJ;","DB02811","Diethylphosphono Group","experimental","unknown"]
[61.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB08712","11-[(MERCAPTOCARBONYL)OXY]UNDECANOIC ACID","experimental","unknown"]
[62.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB08684","O-Decyl Hydrogen Thiocarbonate","experimental","unknown"]
[63.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB08171","11-MERCAPTOUNDECANOIC ACID","experimental","unknown"]
[64.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB07650","DECYL FORMATE","experimental","unknown"]
[65.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB07611","DECANE-1-THIOL","experimental","unknown"]
[66.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB03264","Dodecyl-Coa","experimental","unknown"]
[67.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB03017","Lauric acid","approved, experimental","unknown"]
[68.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Streptomyces lividans","Q9F6D4","BE0002680","P9WNG3",47.0,5.199999999999999E-94,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[69.0,"2.3.1.181","Octanoyltransferase","Mycobacterium tuberculosis","P9WK83","BE0004039","P9WK83",100.0,3.999999999999999E-164,"lipB Rv2217 MTCY190.28","Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. ","FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:16735476}.","CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181; Evidence={ECO:0000255|HAMAP-Rule:MF_00013};","1W66;","DB03600","Capric acid","experimental","unknown"]
[70.0,"2.5.1.68","(2Z,6E)-farnesyl diphosphate synthase","Mycobacterium tuberculosis","P9WFF5","BE0004093","P9WFF5",100.0,0.0,"Rv1086 MTV017.39",null,"FUNCTION: Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl diphosphate, which has a central role in the biosynthesis of the mycobacterial cell wall. {ECO:0000269|PubMed:10816587, ECO:0000269|PubMed:11004176, ECO:0000269|PubMed:11152452}.","CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2Z,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:23300, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:162247; EC=2.5.1.68; Evidence={ECO:0000269|PubMed:11004176};","2VFW;2VG0;2VG1;","DB07780","Farnesyl diphosphate","experimental","unknown"]
[71.0,"2.5.1.68","(2Z,6E)-farnesyl diphosphate synthase","Mycobacterium tuberculosis","P9WFF5","BE0004093","P9WFF5",100.0,0.0,"Rv1086 MTV017.39",null,"FUNCTION: Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl diphosphate, which has a central role in the biosynthesis of the mycobacterial cell wall. {ECO:0000269|PubMed:10816587, ECO:0000269|PubMed:11004176, ECO:0000269|PubMed:11152452}.","CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2Z,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:23300, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:162247; EC=2.5.1.68; Evidence={ECO:0000269|PubMed:11004176};","2VFW;2VG0;2VG1;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[72.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02135","4-{2,6,8-Trioxo-9-[(2R,3S,4R)-2,3,4,5-Tetrahydroxypentyl]-1,2,3,6,8,9-Hexahydro-7h-Purin-7-Yl}Butyl Dihydrogen Phosphate","experimental","unknown"]
[73.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02184","D-1,4-dithiothreitol","experimental","unknown"]
[74.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02290","3-{2,6,8-trioxo-9-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphate","experimental","unknown"]
[75.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB03022","3-{2,6,8-trioxo-9-[(2R,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphate","experimental","unknown"]
[76.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02693","(4S,5S)-1,2-dithiane-4,5-diol","experimental","unknown"]
[77.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02711","4-{2,6,8-Trioxo-9-[(2S,3R,4R)-2,3,4,5-Tetrahydroxypentyl]-1,2,3,6,8,9-Hexahydro-7h-Purin-7-Yl}Butyl Dihydrogen Phosphate","experimental","unknown"]
[78.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB03812","3-{2,6,8-trioxo-9-[(2S,3R,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphate","experimental","unknown"]
[79.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB03973","3-{2,6,8-trioxo-9-[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphate","experimental","unknown"]
[80.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB08016","4-(6-CHLORO-2,4-DIOXO-1,2,3,4-TETRAHYDROPYRIMIDIN-5-YL) BUTYL PHOSPHATE","experimental","unknown"]
[81.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB01692","Dithioerythritol","experimental","unknown"]
[82.0,"2.7.1.33","Pantothenate kinase","Escherichia coli (strain K12)","P0A6I3","BE0001294","P9WPA7",52.1,9.099999999999997E-109,"coaA Rv1092c MTV017.45c","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.33;","2GES;2GET;2GEU;2GEV;2ZS7;2ZS8;2ZS9;2ZSA;2ZSB;2ZSD;2ZSE;2ZSF;3AEZ;3AF0;3AF1;3AF2;3AF3;3AF4;3AVO;3AVP;3AVQ;4BFS;4BFT;4BFU;4BFV;4BFW;4BFX;4BFY;4BFZ;5XLV;5XLW;5XMB;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[83.0,"2.7.1.33","Pantothenate kinase","Escherichia coli (strain K12)","P0A6I3","BE0001294","P9WPA7",52.1,9.099999999999997E-109,"coaA Rv1092c MTV017.45c","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.33;","2GES;2GET;2GEU;2GEV;2ZS7;2ZS8;2ZS9;2ZSA;2ZSB;2ZSD;2ZSE;2ZSF;3AEZ;3AF0;3AF1;3AF2;3AF3;3AF4;3AVO;3AVP;3AVQ;4BFS;4BFT;4BFU;4BFV;4BFW;4BFX;4BFY;4BFZ;5XLV;5XLW;5XMB;","DB01783","Pantothenic acid","approved, nutraceutical, vet_approved","unknown"]
[84.0,"2.7.1.33","Pantothenate kinase","Escherichia coli (strain K12)","P0A6I3","BE0001294","P9WPA7",52.1,9.099999999999997E-109,"coaA Rv1092c MTV017.45c","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.33;","2GES;2GET;2GEU;2GEV;2ZS7;2ZS8;2ZS9;2ZSA;2ZSB;2ZSD;2ZSE;2ZSF;3AEZ;3AF0;3AF1;3AF2;3AF3;3AF4;3AVO;3AVP;3AVQ;4BFS;4BFT;4BFU;4BFV;4BFW;4BFX;4BFY;4BFZ;5XLV;5XLW;5XMB;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[85.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[86.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB03846","5-Hydroxymethyluridine-2'-Deoxy-5'-Monophosphate","experimental","unknown"]
[87.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[88.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB04485","Thymidine","experimental, investigational","unknown"]
[89.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB03666","3'-Azido-3'-Deoxythymidine-5'-Monophosphate","experimental","unknown"]
[90.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[91.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB01643","Thymidine monophosphate","experimental","unknown"]
[92.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X1B3","BE0001839","P9WKG9",34.8,4.4E-28,"ispD Rv3582c MTCY06G11.29c","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};","2XWN;3OKR;3Q7U;3Q80;","DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[93.0,"3.3.1.1","Adenosylhomocysteinase","Mycobacterium tuberculosis","P9WGV3","BE0003776","P9WGV3",100.0,0.0,"ahcY sahH Rv3248c MTCY20B11.23c","Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. ","FUNCTION: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-Rule:MF_00563}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00563};","2ZIZ;2ZJ0;2ZJ1;3CE6;3DHY;","DB07052","5'-S-ethyl-5'-thioadenosine","experimental","unknown"]
[94.0,"3.3.1.1","Adenosylhomocysteinase","Plasmodium falciparum (isolate 3D7)","P50250","BE0009225","P9WGV3",56.0,5.099999999999997E-180,"ahcY sahH Rv3248c MTCY20B11.23c","Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. ","FUNCTION: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-Rule:MF_00563}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00563};","2ZIZ;2ZJ0;2ZJ1;3CE6;3DHY;","DB11638","Artenimol","experimental, investigational","unknown","ligand"]
[95.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Mycobacterium tuberculosis","P9WNS5","BE0001318","P9WNS5",100.0,2.2999999999999996E-103,"dut Rv2697c MTCY05A6.18c","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;","1MQ7;1SIX;1SJN;1SLH;1SM8;1SMC;1SNF;2PY4;3H6D;3HZA;3I93;3LOJ;4GCY;5ECT;5EDD;","DB03800","Deoxyuridine monophosphate","experimental","unknown"]
[96.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Mycobacterium tuberculosis","P9WNS5","BE0001318","P9WNS5",100.0,2.2999999999999996E-103,"dut Rv2697c MTCY05A6.18c","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;","1MQ7;1SIX;1SJN;1SLH;1SM8;1SMC;1SNF;2PY4;3H6D;3HZA;3I93;3LOJ;4GCY;5ECT;5EDD;","DB01965","2'-Deoxyuridine 5'-Alpha,Beta-Imido-Triphosphate","experimental","unknown"]
[97.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Mycobacterium tuberculosis","P9WNS5","BE0001318","P9WNS5",100.0,2.2999999999999996E-103,"dut Rv2697c MTCY05A6.18c","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;","1MQ7;1SIX;1SJN;1SLH;1SM8;1SMC;1SNF;2PY4;3H6D;3HZA;3I93;3LOJ;4GCY;5ECT;5EDD;","DB02333","Deoxyuridine-5'-Triphosphate","experimental","unknown"]
[98.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Mycobacterium tuberculosis","P9WNS5","BE0001318","P9WNS5",100.0,2.2999999999999996E-103,"dut Rv2697c MTCY05A6.18c","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;","1MQ7;1SIX;1SJN;1SLH;1SM8;1SMC;1SNF;2PY4;3H6D;3HZA;3I93;3LOJ;4GCY;5ECT;5EDD;","DB03413","Deoxyuridine-5'-Diphosphate","experimental","unknown"]
[99.0,"4.1.1.11","Aspartate 1-decarboxylase","Shigella flexneri","P0A793","BE0001513","P9WIL3",50.4,1.0E-33,"panD Rv3601c MTCY07H7B.21","Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. ","FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_00446, ECO:0000305|PubMed:12182836}.; FUNCTION: Overexpression of wild-type protein confers resistance to pyrazinoic acid (POA), the active form of the anti-tuberculosis prodrug pyrazinamide (PZA). {ECO:0000269|PubMed:26038753}.","CATALYTIC ACTIVITY: Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00446, ECO:0000269|PubMed:12182836};","2C45;","DB03382","S-oxy-L-cysteine","experimental","unknown"]
[100.0,"4.1.1.11","Aspartate 1-decarboxylase","Shigella flexneri","P0A793","BE0001513","P9WIL3",50.4,1.0E-33,"panD Rv3601c MTCY07H7B.21","Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. ","FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_00446, ECO:0000305|PubMed:12182836}.; FUNCTION: Overexpression of wild-type protein confers resistance to pyrazinoic acid (POA), the active form of the anti-tuberculosis prodrug pyrazinamide (PZA). {ECO:0000269|PubMed:26038753}.","CATALYTIC ACTIVITY: Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00446, ECO:0000269|PubMed:12182836};","2C45;","DB02175","Malonic acid","experimental","unknown"]
[101.0,"4.1.3.36","1,4-Dihydroxy-2-naphthoyl-CoA synthase","Mycobacterium tuberculosis","P9WNP5","BE0002684","P9WNP5",100.0,0.0,"menB Rv0548c","Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7. Quinol/quinone metabolism; menaquinone biosynthesis. ","FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA). {ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628}.","CATALYTIC ACTIVITY: Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57364, ChEBI:CHEBI:58897; EC=4.1.3.36; Evidence={ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:20643650, ECO:0000269|PubMed:21830810};","1Q51;1Q52;1RJM;1RJN;3T8A;3T8B;4QII;4QIJ;","DB03059","Acetoacetyl-CoA","experimental","unknown"]
[102.0,"4.1.3.36","1,4-Dihydroxy-2-naphthoyl-CoA synthase","Mycobacterium tuberculosis","P9WNP5","BE0002684","P9WNP5",100.0,0.0,"menB Rv0548c","Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7. Quinol/quinone metabolism; menaquinone biosynthesis. ","FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA). {ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628}.","CATALYTIC ACTIVITY: Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57364, ChEBI:CHEBI:58897; EC=4.1.3.36; Evidence={ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:20643650, ECO:0000269|PubMed:21830810};","1Q51;1Q52;1RJM;1RJN;3T8A;3T8B;4QII;4QIJ;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[103.0,"4.2.1.10","3-dehydroquinate dehydratase","Mycobacterium tuberculosis","P9WPX7","BE0001857","P9WPX7",100.0,3.6999999999999995E-99,"aroQ aroD Rv2537c MTCY159.19","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10;","1H05;1H0R;1H0S;2DHQ;2XB8;2Y71;2Y76;2Y77;3N59;3N76;3N7A;3N86;3N87;3N8K;3N8N;4B6O;4B6P;4B6Q;4CIV;4CIW;4CIX;4CIY;4CKW;4CKX;4CKY;4CKZ;4CL0;4KI7;4KIJ;4KIU;4KIW;4V0S;","DB02801","2,3-Anhydro-quinic acid","experimental","unknown"]
[104.0,"4.2.1.10","3-dehydroquinate dehydratase","Mycobacterium tuberculosis","P9WPX7","BE0001857","P9WPX7",100.0,3.6999999999999995E-99,"aroQ aroD Rv2537c MTCY159.19","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10;","1H05;1H0R;1H0S;2DHQ;2XB8;2Y71;2Y76;2Y77;3N59;3N76;3N7A;3N86;3N87;3N8K;3N8N;4B6O;4B6P;4B6Q;4CIV;4CIW;4CIX;4CIY;4CKW;4CKX;4CKY;4CKZ;4CL0;4KI7;4KIJ;4KIU;4KIW;4V0S;","DB03739","3-Hydroxyimino Quinic Acid","experimental","unknown"]
[105.0,"4.2.1.113","O-succinylbenzoate-CoA synthase","Thermobifida fusca (strain YX)","Q47Q21","BE0004273","P9WJP3",51.3,5.199999999999999E-86,"menC Rv0553 MTCY25D10.32","Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7. Quinol/quinone metabolism; menaquinone biosynthesis. ","FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000255|HAMAP-Rule:MF_00470}.","CATALYTIC ACTIVITY: Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377, ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113; Evidence={ECO:0000255|HAMAP-Rule:MF_00470};",null,"DB02251","O-Succinylbenzoate","experimental","unknown"]
[106.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)","A0R559","BE0004142","P9WKG5",76.0,3.9999999999999995E-78,"ispF Rv3581c MTCY06G11.28c","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000269|PubMed:20189102}.","CATALYTIC ACTIVITY: Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000269|PubMed:20189102};",null,"DB04714","ISOPENTENYL PYROPHOSPHATE","experimental","unknown"]
[107.0,"4.99.1.1","Ferrochelatase","Bacillus subtilis (strain 168)","P32396","BE0001307","P9WNE3",30.2,2.6E-34,"hemH hemZ Rv1485 MTCY277.06","Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. ","FUNCTION: Involved in the biosynthesis of heme. Catalyzes the ferrous insertion into protoporphyrin IX to form protoheme. {ECO:0000269|PubMed:11948160, ECO:0000269|PubMed:15850757}.","CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;",null,"DB02188","N-Methylmesoporphyrin Containing Copper","experimental","unknown"]
[108.0,"4.99.1.1","Ferrochelatase","Bacillus subtilis (strain 168)","P32396","BE0001307","P9WNE3",30.2,2.6E-34,"hemH hemZ Rv1485 MTCY277.06","Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. ","FUNCTION: Involved in the biosynthesis of heme. Catalyzes the ferrous insertion into protoporphyrin IX to form protoheme. {ECO:0000269|PubMed:11948160, ECO:0000269|PubMed:15850757}.","CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;",null,"DB01911","N-Methylmesoporphyrin","experimental","unknown"]
[109.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Mycobacterium tuberculosis","P9WH11","BE0003322","P9WH11",100.0,2.799999999999999E-148,"rmlC strM Rv3465","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage. {ECO:0000269|PubMed:16472764}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000269|PubMed:16472764};","1PM7;1UPI;2IXC;","DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[110.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB03165","2-Dimethylamino-Ethyl-Diphosphate","experimental","unknown"]
[111.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[112.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[113.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB04170","4-bromo-3-hydroxy-3-methyl butyl diphosphate","experimental","unknown"]
[114.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB01799","4-Hydroxy-3-Methyl Butyl Diphosphate","experimental","unknown"]
[115.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB02480","(S)-4-bromo-3-hydroxy-3-methylbutyl diphosphate","experimental","unknown"]
[116.0,"5.4.99.9","UDP-galactopyranose mutase","Mycobacterium tuberculosis","P9WIQ1","BE0002976","P9WIQ1",100.0,0.0,"glf Rv3809c","Cell wall biogenesis; cell wall polysaccharide biosynthesis. ","FUNCTION: Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is a key building block for cell wall construction in Mycobacterium tuberculosis. {ECO:0000269|PubMed:9692181}.","CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose; Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915; EC=5.4.99.9;","1V0J;4RPG;4RPH;4RPJ;4RPK;4RPL;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[117.0,"5.4.99.9","UDP-galactopyranose mutase","Mycobacterium tuberculosis","P9WIQ1","BE0002976","P9WIQ1",100.0,0.0,"glf Rv3809c","Cell wall biogenesis; cell wall polysaccharide biosynthesis. ","FUNCTION: Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is a key building block for cell wall construction in Mycobacterium tuberculosis. {ECO:0000269|PubMed:9692181}.","CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose; Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915; EC=5.4.99.9;","1V0J;4RPG;4RPH;4RPJ;4RPK;4RPL;","DB03709","Bicine","experimental","unknown"]
[118.0,"5.4.99.9","UDP-galactopyranose mutase","Escherichia coli (strain K12)","P37747","BE0001720","P9WIQ1",43.5,6.599999999999999E-102,"glf Rv3809c","Cell wall biogenesis; cell wall polysaccharide biosynthesis. ","FUNCTION: Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is a key building block for cell wall construction in Mycobacterium tuberculosis. {ECO:0000269|PubMed:9692181}.","CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose; Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915; EC=5.4.99.9;","1V0J;4RPG;4RPH;4RPJ;4RPK;4RPL;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[119.0,"6.3.1.2","Glutamine synthetase 1","Mycobacterium tuberculosis","P9WN39","BE0002555","P9WN39",100.0,0.0,"glnA1 glnA Rv2220 MTCY190.31 MTCY427.01",null,"FUNCTION: Involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:7937767, PubMed:12819079). Also able to use GTP (PubMed:7937767). D-glutamate is a poor substrate, and DL-glutamate shows about 50% of the standard specific activity (PubMed:7937767). Also plays a key role in controlling the ammonia levels within infected host cells and so contributes to the pathogens capacity to inhibit phagosome acidification and phagosome-lysosome fusion (PubMed:7937767, PubMed:12819079). Involved in cell wall biosynthesis via the production of the major component poly-L-glutamine (PLG) (PubMed:7937767, PubMed:10618433). PLG synthesis in the cell wall occurs only in nitrogen limiting conditions and on the contrary high nitrogen conditions inhibit PLG synthesis (Probable). {ECO:0000269|PubMed:10618433, ECO:0000269|PubMed:12819079, ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:9278431}.","CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:19695264};","1HTO;1HTQ;2BVC;2WGS;2WHI;3ZXR;3ZXV;4ACF;4XYC;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[120.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","P9WIL5",100.0,0.0,"panC Rv3602c MTCY07H7B.20","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000269|PubMed:11669627}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000269|PubMed:12717031};","1MOP;1N2B;1N2E;1N2G;1N2H;1N2I;1N2J;1N2O;2A7X;2A84;2A86;2A88;3COV;3COW;3COY;3COZ;3IMC;3IME;3IMG;3IOB;3IOC;3IOD;3IOE;3ISJ;3IUB;3IUE;3IVC;3IVG;3IVX;3LE8;4DDH;4DDK;4DDM;4DE5;4EF6;4EFK;4FZJ;4G5F;4G5Y;","DB03107","Beta-Alanine","experimental","unknown"]
[121.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","P9WIL5",100.0,0.0,"panC Rv3602c MTCY07H7B.20","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000269|PubMed:11669627}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000269|PubMed:12717031};","1MOP;1N2B;1N2E;1N2G;1N2H;1N2I;1N2J;1N2O;2A7X;2A84;2A86;2A88;3COV;3COW;3COY;3COZ;3IMC;3IME;3IMG;3IOB;3IOC;3IOD;3IOE;3ISJ;3IUB;3IUE;3IVC;3IVG;3IVX;3LE8;4DDH;4DDK;4DDM;4DE5;4EF6;4EFK;4FZJ;4G5F;4G5Y;","DB02694","Pantoyl Adenylate","experimental","unknown"]
[122.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","P9WIL5",100.0,0.0,"panC Rv3602c MTCY07H7B.20","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000269|PubMed:11669627}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000269|PubMed:12717031};","1MOP;1N2B;1N2E;1N2G;1N2H;1N2I;1N2J;1N2O;2A7X;2A84;2A86;2A88;3COV;3COW;3COY;3COZ;3IMC;3IME;3IMG;3IOB;3IOC;3IOD;3IOE;3ISJ;3IUB;3IUE;3IVC;3IVG;3IVX;3LE8;4DDH;4DDK;4DDM;4DE5;4EF6;4EFK;4FZJ;4G5F;4G5Y;","DB01930","2,4-Dihydroxy-3,3-Dimethyl-Butyrate","experimental","unknown"]
[123.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","P9WIL5",100.0,0.0,"panC Rv3602c MTCY07H7B.20","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000269|PubMed:11669627}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000269|PubMed:12717031};","1MOP;1N2B;1N2E;1N2G;1N2H;1N2I;1N2J;1N2O;2A7X;2A84;2A86;2A88;3COV;3COW;3COY;3COZ;3IMC;3IME;3IMG;3IOB;3IOC;3IOD;3IOE;3ISJ;3IUB;3IUE;3IVC;3IVG;3IVX;3LE8;4DDH;4DDK;4DDM;4DE5;4EF6;4EFK;4FZJ;4G5F;4G5Y;","DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]

{"sheet":"M. tuberculosis FBA-only","index":15,"n_rows":125,"n_cols":19,"rows_kept":125,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.17.4.1","Ribonucleoside-diphosphate reductase 2 subunit alpha","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","Q08698","BE0001782","P9WH75",72.9,0.0,"nrdE Rv3051c MTV012.66c","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. When coexpressed in E.coli with nrdF2 the 2 proteins complement a temperature-sensitive E.coli mutant, however coexpression with nrdF1 does not complement. {ECO:0000269|PubMed:9335290}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000269|PubMed:9335290};",null,"DB03258","2'-Deoxycytidine 5'-triphosphate","experimental","unknown"]
[1.0,"1.17.4.1","Ribonucleoside-diphosphate reductase 2 subunit alpha","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","Q08698","BE0001782","P9WH75",72.9,0.0,"nrdE Rv3051c MTV012.66c","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. When coexpressed in E.coli with nrdF2 the 2 proteins complement a temperature-sensitive E.coli mutant, however coexpression with nrdF1 does not complement. {ECO:0000269|PubMed:9335290}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000269|PubMed:9335290};",null,"DB03222","dATP","experimental","unknown"]
[2.0,"1.17.4.1","Ribonucleoside-diphosphate reductase 2 subunit alpha","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","Q08698","BE0001782","P9WH75",72.9,0.0,"nrdE Rv3051c MTV012.66c","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. When coexpressed in E.coli with nrdF2 the 2 proteins complement a temperature-sensitive E.coli mutant, however coexpression with nrdF1 does not complement. {ECO:0000269|PubMed:9335290}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000269|PubMed:9335290};",null,"DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[3.0,"1.17.4.1","Ribonucleoside-diphosphate reductase subunit beta","Mycobacterium leprae (strain TN)","Q9CBQ2","BE0003267","P9WH73",71.2,1.5999999999999994E-166,"nrdF1 Rv1981c MTCY39.38","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity). Two genes for this protein are present in M.tuberculosis; this is thought to not be the active form. When coexpressed in E.coli with nrdE the 2 proteins do not complement a temperature-sensitive E.coli mutant, whereas the other gene (nrdF2) does complement. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10014};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[4.0,"1.17.4.1","Ribonucleoside-diphosphate reductase subunit beta","Mycobacterium leprae (strain TN)","Q9CBQ2","BE0003267","P9WH71",93.5,0.0,"nrdF2 Rv3048c","Genetic information processing; DNA replication. ","FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Two genes for this protein are present in M.tuberculosis; this is the active form. When coexpressed in E.coli with nrdE the 2 proteins complement a temperature-sensitive E.coli mutant. {ECO:0000269|PubMed:9335290}.","CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10014, ECO:0000269|PubMed:9335290};","1UZR;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[5.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q79FX8",50.0,1.1999999999999999E-95,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[6.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q79FX8",50.0,1.1999999999999999E-95,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[7.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB1",51.5,1.1999999999999997E-96,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[8.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB1",51.5,1.1999999999999997E-96,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[9.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P0CH91",51.9,7.699999999999997E-102,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[10.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P0CH91",51.9,7.699999999999997E-102,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[11.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q6MX39",53.4,5.299999999999999E-103,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[12.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q6MX39",53.4,5.299999999999999E-103,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[13.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB7",55.7,3.5999999999999996E-106,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[14.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB7",55.7,3.5999999999999996E-106,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[15.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q79FX6",55.9,8.1E-110,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[16.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","Q79FX6",55.9,8.1E-110,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[17.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB3",58.4,1.9999999999999994E-115,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[18.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB3",58.4,1.9999999999999994E-115,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[19.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB5",100.0,0.0,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB04221","Didecyldimethylammonium","approved, experimental","unknown"]
[20.0,"2.1.1.79","Cyclopropane mycolic acid synthase 2","Mycobacterium tuberculosis","P9WPB5","BE0001211","P9WPB5",100.0,0.0,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[21.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB1",53.4,1.6999999999999995E-102,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[22.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB1",53.4,1.6999999999999995E-102,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[23.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q6MX39",55.2,4.899999999999999E-107,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[24.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q6MX39",55.2,4.899999999999999E-107,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[25.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB5",55.9,7.699999999999997E-110,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01718","Cetrimonium","approved","unknown"]
[26.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB5",55.9,7.699999999999997E-110,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[27.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q79FX8",57.0,7.499999999999997E-110,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01718","Cetrimonium","approved","unknown"]
[28.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q79FX8",57.0,7.499999999999997E-110,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[29.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P0CH91",69.1,1.9999999999999995E-141,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[30.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P0CH91",69.1,1.9999999999999995E-141,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[31.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB7",73.5,2.1999999999999995E-155,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01718","Cetrimonium","approved","unknown"]
[32.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB7",73.5,2.1999999999999995E-155,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[33.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q79FX6",100.0,0.0,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01718","Cetrimonium","approved","unknown"]
[34.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","Q79FX6",100.0,0.0,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[35.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB3",73.1,4.299999999999998E-146,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01718","Cetrimonium","approved","unknown"]
[36.0,"2.1.1.79","Cyclopropane mycolic acid synthase MmaA2","Mycobacterium tuberculosis","Q79FX6","BE0002512","P9WPB3",73.1,4.299999999999998E-146,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[37.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","Q79FX8",55.6,7.599999999999998E-105,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[38.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P9WPB1",54.6,4.599999999999999E-105,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[39.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","Q6MX39",57.4,6.399999999999998E-110,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[40.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P9WPB5",58.4,1.8999999999999997E-115,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[41.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P0CH91",64.3,5.799999999999998E-129,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[42.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P9WPB3",100.0,0.0,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[43.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","P9WPB7",72.8,9.599999999999997E-150,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[44.0,"2.1.1.79","Cyclopropane mycolic acid synthase 3","Mycobacterium tuberculosis","P9WPB3","BE0002521","Q79FX6",73.1,4.299999999999998E-146,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01752","S-adenosyl-L-homocysteine","experimental","unknown"]
[45.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P9WPB7",100.0,0.0,"cmaA1 cma1 CMAS-1 Rv3392c MTV004.50","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KP9;1KPG;1KPH;","DB01718","Cetrimonium","approved","unknown"]
[46.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","Q6MX39",56.7,6.399999999999998E-110,"umaA Rv0469 LH57_02505",null,"FUNCTION: Methyltransferase that modifies short-chain fatty acids. In vitro, catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of phospholipid-linked oleic acid to produce tuberculostearic acid (10-methylstearic-acid or TSA). {ECO:0000269|PubMed:23435098}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[47.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","Q79FX6",73.5,2.1999999999999995E-155,"mmaA2 mma2 Rv0644c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:12502719, ECO:0000269|PubMed:20472794}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1TPY;","DB01718","Cetrimonium","approved","unknown"]
[48.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P9WPB3",72.8,9.599999999999997E-150,"pcaA cma3 cmaA3 CMAS-3 Rv0470c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the phagosome maturation block (PMB). Catalyzes the conversion of a double bond to a cyclopropane ring at the proximal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:10882107, ECO:0000269|PubMed:22621931}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79; Evidence={ECO:0000269|PubMed:22621931};","1L1E;","DB01718","Cetrimonium","approved","unknown"]
[49.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P0CH91",68.6,3.7999999999999986E-139,"mmaA3 mma3 Rv0643c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether. {ECO:0000269|PubMed:10852869, ECO:0000269|PubMed:9781881}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[50.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P9WPB1",57.0,4.4999999999999995E-110,"mmaA1 mma1 Rv0645c MTCY20H10.26c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the conversion of a cis-olefin into a trans-olefin with concomitant introduction of an allylic methyl branch at the proximal position of the precursor to both the methoxy and ketomycolic acids. It directly affects the cis- to trans ratio and indirectly affects the keto to methoxy ratio. {ECO:0000269|PubMed:20472794, ECO:0000269|PubMed:9092547}.",null,null,"DB01718","Cetrimonium","approved","unknown"]
[51.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","P9WPB5",55.7,3.4E-106,"cmaA2 cma2 CMAS-2 Rv0503c MTCY20G9.30c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. {ECO:0000269|PubMed:11092877, ECO:0000269|PubMed:7592990}.","CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;","1KPI;3HEM;","DB01718","Cetrimonium","approved","unknown"]
[52.0,"2.1.1.79","Cyclopropane mycolic acid synthase 1","Mycobacterium tuberculosis","P9WPB7","BE0003738","Q79FX8",58.7,8.999999999999999E-116,"mmaA4 hma mma4 Rv0642c","Lipid metabolism; mycolic acid biosynthesis. ","FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxy-mycolate and keto-mycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position. Involved in the activation of the antitubercular drug thiacetazone (TAC). {ECO:0000269|PubMed:10844652, ECO:0000269|PubMed:12473649}.",null,"2FK7;2FK8;3HA3;3HA5;3HA7;","DB01718","Cetrimonium","approved","unknown"]
[53.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQP3",67.3,1.4999999999999994E-165,"fbpA mpt44 Rv3804c MTV026.09c",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan, and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA. {ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:21819455, ECO:0000269|PubMed:3141278, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:21819455}; CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; Evidence={ECO:0000269|PubMed:21819455};","1SFR;","DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[54.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQP3",67.3,1.4999999999999994E-165,"fbpA mpt44 Rv3804c MTV026.09c",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan, and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA. {ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:21819455, ECO:0000269|PubMed:3141278, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:21819455}; CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; Evidence={ECO:0000269|PubMed:21819455};","1SFR;","DB02811","Diethylphosphono Group","experimental","unknown"]
[55.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQP1",71.6,7.199999999999997E-163,"fbpB Rv1886c MTCY180.32",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. {ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:3141278, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;","1F0N;1F0P;5TRZ;5TS1;","DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[56.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQP1",71.6,7.199999999999997E-163,"fbpB Rv1886c MTCY180.32",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. {ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:3141278, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;","1F0N;1F0P;5TRZ;5TS1;","DB02811","Diethylphosphono Group","experimental","unknown"]
[57.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQN7",40.5,8.199999999999998E-65,"mpt51 fbpC1 fbpD mpb51 Rv3803c MTV026.08c",null,"FUNCTION: May have a role in host tissue attachment, whereby ligands may include the serum protein fibronectin and small sugars. {ECO:0000269|PubMed:14672660}.",null,"1R88;","DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[58.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQN7",40.5,8.199999999999998E-65,"mpt51 fbpC1 fbpD mpb51 Rv3803c MTV026.08c",null,"FUNCTION: May have a role in host tissue attachment, whereby ligands may include the serum protein fibronectin and small sugars. {ECO:0000269|PubMed:14672660}.",null,"1R88;","DB02811","Diethylphosphono Group","experimental","unknown"]
[59.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQN9",100.0,0.0,"fbpC mpt45 Rv0129c MTCI5.03c",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria to fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. {ECO:0000269|PubMed:1830294, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122;","1DQY;1DQZ;1VA5;3HRH;4MQL;4MQM;4QDO;4QDT;4QDU;4QDX;4QDZ;4QE3;4QEK;5KWI;5KWJ;5OCJ;","DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[60.0,"2.3.1.122","Diacylglycerol acyltransferase/mycolyltransferase Ag85C","Mycobacterium tuberculosis","P9WQN9","BE0001688","P9WQN9",100.0,0.0,"fbpC mpt45 Rv0129c MTCI5.03c",null,"FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria to fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. {ECO:0000269|PubMed:1830294, ECO:0000269|PubMed:9162010}.","CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122;","1DQY;1DQZ;1VA5;3HRH;4MQL;4MQM;4QDO;4QDT;4QDU;4QDX;4QDZ;4QE3;4QEK;5KWI;5KWJ;5OCJ;","DB02811","Diethylphosphono Group","experimental","unknown"]
[61.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB08712","11-[(MERCAPTOCARBONYL)OXY]UNDECANOIC ACID","experimental","unknown"]
[62.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB08684","O-Decyl Hydrogen Thiocarbonate","experimental","unknown"]
[63.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB08171","11-MERCAPTOUNDECANOIC ACID","experimental","unknown"]
[64.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB07650","DECYL FORMATE","experimental","unknown"]
[65.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB07611","DECANE-1-THIOL","experimental","unknown"]
[66.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB03264","Dodecyl-Coa","experimental","unknown"]
[67.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Mycobacterium tuberculosis","P9WNG3","BE0001723","P9WNG3",100.0,0.0,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB03017","Lauric acid","approved, experimental","unknown"]
[68.0,"2.3.1.180","3-oxoacyl-[acyl-carrier-protein] synthase 3","Streptomyces lividans","Q9F6D4","BE0002680","P9WNG3",47.0,5.199999999999999E-94,"fabH Rv0533c MTCY25D10.12c","Lipid metabolism; fatty acid biosynthesis. ","FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. {ECO:0000269|PubMed:10840036}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};","1HZP;1M1M;1U6E;1U6S;2AHB;2AJ9;2QNX;2QNY;2QNZ;2QO0;2QO1;2QX1;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[69.0,"2.3.1.181","Octanoyltransferase","Mycobacterium tuberculosis","P9WK83","BE0004039","P9WK83",100.0,3.999999999999999E-164,"lipB Rv2217 MTCY190.28","Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. ","FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:16735476}.","CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181; Evidence={ECO:0000255|HAMAP-Rule:MF_00013};","1W66;","DB03600","Capric acid","experimental","unknown"]
[70.0,"2.5.1.68","(2Z,6E)-farnesyl diphosphate synthase","Mycobacterium tuberculosis","P9WFF5","BE0004093","P9WFF5",100.0,0.0,"Rv1086 MTV017.39",null,"FUNCTION: Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl diphosphate, which has a central role in the biosynthesis of the mycobacterial cell wall. {ECO:0000269|PubMed:10816587, ECO:0000269|PubMed:11004176, ECO:0000269|PubMed:11152452}.","CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2Z,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:23300, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:162247; EC=2.5.1.68; Evidence={ECO:0000269|PubMed:11004176};","2VFW;2VG0;2VG1;","DB07780","Farnesyl diphosphate","experimental","unknown"]
[71.0,"2.5.1.68","(2Z,6E)-farnesyl diphosphate synthase","Mycobacterium tuberculosis","P9WFF5","BE0004093","P9WFF5",100.0,0.0,"Rv1086 MTV017.39",null,"FUNCTION: Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl diphosphate, which has a central role in the biosynthesis of the mycobacterial cell wall. {ECO:0000269|PubMed:10816587, ECO:0000269|PubMed:11004176, ECO:0000269|PubMed:11152452}.","CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2Z,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:23300, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:162247; EC=2.5.1.68; Evidence={ECO:0000269|PubMed:11004176};","2VFW;2VG0;2VG1;","DB02552","Geranyl Diphosphate","experimental","unknown"]
[72.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02135","4-{2,6,8-Trioxo-9-[(2R,3S,4R)-2,3,4,5-Tetrahydroxypentyl]-1,2,3,6,8,9-Hexahydro-7h-Purin-7-Yl}Butyl Dihydrogen Phosphate","experimental","unknown"]
[73.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02184","D-1,4-dithiothreitol","experimental","unknown"]
[74.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02290","3-{2,6,8-trioxo-9-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphate","experimental","unknown"]
[75.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB03022","3-{2,6,8-trioxo-9-[(2R,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphate","experimental","unknown"]
[76.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02693","(4S,5S)-1,2-dithiane-4,5-diol","experimental","unknown"]
[77.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB02711","4-{2,6,8-Trioxo-9-[(2S,3R,4R)-2,3,4,5-Tetrahydroxypentyl]-1,2,3,6,8,9-Hexahydro-7h-Purin-7-Yl}Butyl Dihydrogen Phosphate","experimental","unknown"]
[78.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB03812","3-{2,6,8-trioxo-9-[(2S,3R,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphate","experimental","unknown"]
[79.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB03973","3-{2,6,8-trioxo-9-[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphate","experimental","unknown"]
[80.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB08016","4-(6-CHLORO-2,4-DIOXO-1,2,3,4-TETRAHYDROPYRIMIDIN-5-YL) BUTYL PHOSPHATE","experimental","unknown"]
[81.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Mycobacterium tuberculosis","P9WHE9","BE0001270","P9WHE9",100.0,2.399999999999999E-108,"ribH Rv1416 MTCY21B4.34","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:15723519}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;","1W19;1W29;2C92;2C94;2C97;2C9B;2C9D;2VI5;","DB01692","Dithioerythritol","experimental","unknown"]
[82.0,"2.7.1.33","Pantothenate kinase","Escherichia coli (strain K12)","P0A6I3","BE0001294","P9WPA7",52.1,9.099999999999997E-109,"coaA Rv1092c MTV017.45c","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.33;","2GES;2GET;2GEU;2GEV;2ZS7;2ZS8;2ZS9;2ZSA;2ZSB;2ZSD;2ZSE;2ZSF;3AEZ;3AF0;3AF1;3AF2;3AF3;3AF4;3AVO;3AVP;3AVQ;4BFS;4BFT;4BFU;4BFV;4BFW;4BFX;4BFY;4BFZ;5XLV;5XLW;5XMB;","DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[83.0,"2.7.1.33","Pantothenate kinase","Escherichia coli (strain K12)","P0A6I3","BE0001294","P9WPA7",52.1,9.099999999999997E-109,"coaA Rv1092c MTV017.45c","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.33;","2GES;2GET;2GEU;2GEV;2ZS7;2ZS8;2ZS9;2ZSA;2ZSB;2ZSD;2ZSE;2ZSF;3AEZ;3AF0;3AF1;3AF2;3AF3;3AF4;3AVO;3AVP;3AVQ;4BFS;4BFT;4BFU;4BFV;4BFW;4BFX;4BFY;4BFZ;5XLV;5XLW;5XMB;","DB01783","Pantothenic acid","approved, nutraceutical, vet_approved","unknown"]
[84.0,"2.7.1.33","Pantothenate kinase","Escherichia coli (strain K12)","P0A6I3","BE0001294","P9WPA7",52.1,9.099999999999997E-109,"coaA Rv1092c MTV017.45c","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.33;","2GES;2GET;2GEU;2GEV;2ZS7;2ZS8;2ZS9;2ZSA;2ZSB;2ZSD;2ZSE;2ZSF;3AEZ;3AF0;3AF1;3AF2;3AF3;3AF4;3AVO;3AVP;3AVQ;4BFS;4BFT;4BFU;4BFV;4BFW;4BFX;4BFY;4BFZ;5XLV;5XLW;5XMB;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[85.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB03280","P1-(5'-Adenosyl)P5-(5'-Thymidyl)Pentaphosphate","experimental","unknown"]
[86.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB03846","5-Hydroxymethyluridine-2'-Deoxy-5'-Monophosphate","experimental","unknown"]
[87.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[88.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB04485","Thymidine","experimental, investigational","unknown"]
[89.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB03666","3'-Azido-3'-Deoxythymidine-5'-Monophosphate","experimental","unknown"]
[90.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB02452","Thymidine-5'-Triphosphate","experimental","unknown"]
[91.0,"2.7.4.9","Thymidylate kinase","Mycobacterium tuberculosis","P9WKE1","BE0001218","P9WKE1",100.0,7.299999999999997E-150,"tmk Rv3247c","Pyrimidine metabolism; dTTP biosynthesis. ","FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.","CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9;","1G3U;1GSI;1GTV;1MRN;1MRS;1N5I;1N5J;1N5K;1N5L;1W2G;1W2H;4UNN;4UNP;4UNQ;4UNR;4UNS;5NQ5;5NR7;5NRN;5NRQ;","DB01643","Thymidine monophosphate","experimental","unknown"]
[92.0,"2.7.7.60","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X1B3","BE0001839","P9WKG9",34.8,4.4E-28,"ispD Rv3582c MTCY06G11.29c","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. ","FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.","CATALYTIC ACTIVITY: Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; Evidence={ECO:0000255|HAMAP-Rule:MF_00108};","2XWN;3OKR;3Q7U;3Q80;","DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[93.0,"3.3.1.1","Adenosylhomocysteinase","Mycobacterium tuberculosis","P9WGV3","BE0003776","P9WGV3",100.0,0.0,"ahcY sahH Rv3248c MTCY20B11.23c","Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. ","FUNCTION: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-Rule:MF_00563}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00563};","2ZIZ;2ZJ0;2ZJ1;3CE6;3DHY;","DB07052","5'-S-ethyl-5'-thioadenosine","experimental","unknown"]
[94.0,"3.3.1.1","Adenosylhomocysteinase","Plasmodium falciparum (isolate 3D7)","P50250","BE0009225","P9WGV3",56.0,5.099999999999997E-180,"ahcY sahH Rv3248c MTCY20B11.23c","Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. ","FUNCTION: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-Rule:MF_00563}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00563};","2ZIZ;2ZJ0;2ZJ1;3CE6;3DHY;","DB11638","Artenimol","experimental, investigational","unknown","ligand"]
[95.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Mycobacterium tuberculosis","P9WNS5","BE0001318","P9WNS5",100.0,2.2999999999999996E-103,"dut Rv2697c MTCY05A6.18c","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;","1MQ7;1SIX;1SJN;1SLH;1SM8;1SMC;1SNF;2PY4;3H6D;3HZA;3I93;3LOJ;4GCY;5ECT;5EDD;","DB03800","Deoxyuridine monophosphate","experimental","unknown"]
[96.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Mycobacterium tuberculosis","P9WNS5","BE0001318","P9WNS5",100.0,2.2999999999999996E-103,"dut Rv2697c MTCY05A6.18c","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;","1MQ7;1SIX;1SJN;1SLH;1SM8;1SMC;1SNF;2PY4;3H6D;3HZA;3I93;3LOJ;4GCY;5ECT;5EDD;","DB01965","2'-Deoxyuridine 5'-Alpha,Beta-Imido-Triphosphate","experimental","unknown"]
[97.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Mycobacterium tuberculosis","P9WNS5","BE0001318","P9WNS5",100.0,2.2999999999999996E-103,"dut Rv2697c MTCY05A6.18c","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;","1MQ7;1SIX;1SJN;1SLH;1SM8;1SMC;1SNF;2PY4;3H6D;3HZA;3I93;3LOJ;4GCY;5ECT;5EDD;","DB02333","Deoxyuridine-5'-Triphosphate","experimental","unknown"]
[98.0,"3.6.1.23","Deoxyuridine 5'-triphosphate nucleotidohydrolase","Mycobacterium tuberculosis","P9WNS5","BE0001318","P9WNS5",100.0,2.2999999999999996E-103,"dut Rv2697c MTCY05A6.18c","Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. ","FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.","CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;","1MQ7;1SIX;1SJN;1SLH;1SM8;1SMC;1SNF;2PY4;3H6D;3HZA;3I93;3LOJ;4GCY;5ECT;5EDD;","DB03413","Deoxyuridine-5'-Diphosphate","experimental","unknown"]
[99.0,"4.1.1.11","Aspartate 1-decarboxylase","Shigella flexneri","P0A793","BE0001513","P9WIL3",50.4,1.0E-33,"panD Rv3601c MTCY07H7B.21","Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. ","FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_00446, ECO:0000305|PubMed:12182836}.; FUNCTION: Overexpression of wild-type protein confers resistance to pyrazinoic acid (POA), the active form of the anti-tuberculosis prodrug pyrazinamide (PZA). {ECO:0000269|PubMed:26038753}.","CATALYTIC ACTIVITY: Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00446, ECO:0000269|PubMed:12182836};","2C45;","DB03382","S-oxy-L-cysteine","experimental","unknown"]
[100.0,"4.1.1.11","Aspartate 1-decarboxylase","Shigella flexneri","P0A793","BE0001513","P9WIL3",50.4,1.0E-33,"panD Rv3601c MTCY07H7B.21","Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. ","FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_00446, ECO:0000305|PubMed:12182836}.; FUNCTION: Overexpression of wild-type protein confers resistance to pyrazinoic acid (POA), the active form of the anti-tuberculosis prodrug pyrazinamide (PZA). {ECO:0000269|PubMed:26038753}.","CATALYTIC ACTIVITY: Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00446, ECO:0000269|PubMed:12182836};","2C45;","DB02175","Malonic acid","experimental","unknown"]
[101.0,"4.1.3.36","1,4-Dihydroxy-2-naphthoyl-CoA synthase","Mycobacterium tuberculosis","P9WNP5","BE0002684","P9WNP5",100.0,0.0,"menB Rv0548c","Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7. Quinol/quinone metabolism; menaquinone biosynthesis. ","FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA). {ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628}.","CATALYTIC ACTIVITY: Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57364, ChEBI:CHEBI:58897; EC=4.1.3.36; Evidence={ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:20643650, ECO:0000269|PubMed:21830810};","1Q51;1Q52;1RJM;1RJN;3T8A;3T8B;4QII;4QIJ;","DB03059","Acetoacetyl-CoA","experimental","unknown"]
[102.0,"4.1.3.36","1,4-Dihydroxy-2-naphthoyl-CoA synthase","Mycobacterium tuberculosis","P9WNP5","BE0002684","P9WNP5",100.0,0.0,"menB Rv0548c","Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7. Quinol/quinone metabolism; menaquinone biosynthesis. ","FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA). {ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628}.","CATALYTIC ACTIVITY: Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57364, ChEBI:CHEBI:58897; EC=4.1.3.36; Evidence={ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:20643650, ECO:0000269|PubMed:21830810};","1Q51;1Q52;1RJM;1RJN;3T8A;3T8B;4QII;4QIJ;","DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[103.0,"4.2.1.10","3-dehydroquinate dehydratase","Mycobacterium tuberculosis","P9WPX7","BE0001857","P9WPX7",100.0,3.6999999999999995E-99,"aroQ aroD Rv2537c MTCY159.19","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10;","1H05;1H0R;1H0S;2DHQ;2XB8;2Y71;2Y76;2Y77;3N59;3N76;3N7A;3N86;3N87;3N8K;3N8N;4B6O;4B6P;4B6Q;4CIV;4CIW;4CIX;4CIY;4CKW;4CKX;4CKY;4CKZ;4CL0;4KI7;4KIJ;4KIU;4KIW;4V0S;","DB02801","2,3-Anhydro-quinic acid","experimental","unknown"]
[104.0,"4.2.1.10","3-dehydroquinate dehydratase","Mycobacterium tuberculosis","P9WPX7","BE0001857","P9WPX7",100.0,3.6999999999999995E-99,"aroQ aroD Rv2537c MTCY159.19","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. {ECO:0000250}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10;","1H05;1H0R;1H0S;2DHQ;2XB8;2Y71;2Y76;2Y77;3N59;3N76;3N7A;3N86;3N87;3N8K;3N8N;4B6O;4B6P;4B6Q;4CIV;4CIW;4CIX;4CIY;4CKW;4CKX;4CKY;4CKZ;4CL0;4KI7;4KIJ;4KIU;4KIW;4V0S;","DB03739","3-Hydroxyimino Quinic Acid","experimental","unknown"]
[105.0,"4.2.1.113","O-succinylbenzoate-CoA synthase","Thermobifida fusca (strain YX)","Q47Q21","BE0004273","P9WJP3",51.3,5.199999999999999E-86,"menC Rv0553 MTCY25D10.32","Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7. Quinol/quinone metabolism; menaquinone biosynthesis. ","FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000255|HAMAP-Rule:MF_00470}.","CATALYTIC ACTIVITY: Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377, ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113; Evidence={ECO:0000255|HAMAP-Rule:MF_00470};",null,"DB02251","O-Succinylbenzoate","experimental","unknown"]
[106.0,"4.6.1.12","2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)","A0R559","BE0004142","P9WKG5",76.0,3.9999999999999995E-78,"ispF Rv3581c MTCY06G11.28c","Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. ","FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). {ECO:0000269|PubMed:20189102}.","CATALYTIC ACTIVITY: Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; Evidence={ECO:0000269|PubMed:20189102};",null,"DB04714","ISOPENTENYL PYROPHOSPHATE","experimental","unknown"]
[107.0,"4.99.1.1","Ferrochelatase","Bacillus subtilis (strain 168)","P32396","BE0001307","P9WNE3",30.2,2.6E-34,"hemH hemZ Rv1485 MTCY277.06","Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. ","FUNCTION: Involved in the biosynthesis of heme. Catalyzes the ferrous insertion into protoporphyrin IX to form protoheme. {ECO:0000269|PubMed:11948160, ECO:0000269|PubMed:15850757}.","CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;",null,"DB02188","N-Methylmesoporphyrin Containing Copper","experimental","unknown"]
[108.0,"4.99.1.1","Ferrochelatase","Bacillus subtilis (strain 168)","P32396","BE0001307","P9WNE3",30.2,2.6E-34,"hemH hemZ Rv1485 MTCY277.06","Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. ","FUNCTION: Involved in the biosynthesis of heme. Catalyzes the ferrous insertion into protoporphyrin IX to form protoheme. {ECO:0000269|PubMed:11948160, ECO:0000269|PubMed:15850757}.","CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;",null,"DB01911","N-Methylmesoporphyrin","experimental","unknown"]
[109.0,"5.1.3.13","dTDP-4-dehydrorhamnose 3,5-epimerase","Mycobacterium tuberculosis","P9WH11","BE0003322","P9WH11",100.0,2.799999999999999E-148,"rmlC strM Rv3465","Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. ","FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage. {ECO:0000269|PubMed:16472764}.","CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649, ChEBI:CHEBI:62830; EC=5.1.3.13; Evidence={ECO:0000269|PubMed:16472764};","1PM7;1UPI;2IXC;","DB04530","S,S-(2-Hydroxyethyl)Thiocysteine","experimental","unknown"]
[110.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB03165","2-Dimethylamino-Ethyl-Diphosphate","experimental","unknown"]
[111.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB03366","Imidazole","experimental, investigational","unknown"]
[112.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[113.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB04170","4-bromo-3-hydroxy-3-methyl butyl diphosphate","experimental","unknown"]
[114.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB01799","4-Hydroxy-3-Methyl Butyl Diphosphate","experimental","unknown"]
[115.0,"5.3.3.2","Isopentenyl-diphosphate Delta-isomerase","Escherichia coli (strain K12)","Q46822","BE0001417","P9WKK5",46.9,6.9000000000000004E-40,"idi Rv1745c MTCY04C12.29c MTCY28.08c","Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. ","FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};",null,"DB02480","(S)-4-bromo-3-hydroxy-3-methylbutyl diphosphate","experimental","unknown"]
[116.0,"5.4.99.9","UDP-galactopyranose mutase","Mycobacterium tuberculosis","P9WIQ1","BE0002976","P9WIQ1",100.0,0.0,"glf Rv3809c","Cell wall biogenesis; cell wall polysaccharide biosynthesis. ","FUNCTION: Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is a key building block for cell wall construction in Mycobacterium tuberculosis. {ECO:0000269|PubMed:9692181}.","CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose; Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915; EC=5.4.99.9;","1V0J;4RPG;4RPH;4RPJ;4RPK;4RPL;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[117.0,"5.4.99.9","UDP-galactopyranose mutase","Mycobacterium tuberculosis","P9WIQ1","BE0002976","P9WIQ1",100.0,0.0,"glf Rv3809c","Cell wall biogenesis; cell wall polysaccharide biosynthesis. ","FUNCTION: Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is a key building block for cell wall construction in Mycobacterium tuberculosis. {ECO:0000269|PubMed:9692181}.","CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose; Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915; EC=5.4.99.9;","1V0J;4RPG;4RPH;4RPJ;4RPK;4RPL;","DB03709","Bicine","experimental","unknown"]
[118.0,"5.4.99.9","UDP-galactopyranose mutase","Escherichia coli (strain K12)","P37747","BE0001720","P9WIQ1",43.5,6.599999999999999E-102,"glf Rv3809c","Cell wall biogenesis; cell wall polysaccharide biosynthesis. ","FUNCTION: Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is a key building block for cell wall construction in Mycobacterium tuberculosis. {ECO:0000269|PubMed:9692181}.","CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose; Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915; EC=5.4.99.9;","1V0J;4RPG;4RPH;4RPJ;4RPK;4RPL;","DB03147","Flavin adenine dinucleotide","approved","unknown"]
[119.0,"6.3.1.2","Glutamine synthetase 1","Mycobacterium tuberculosis","P9WN39","BE0002555","P9WN39",100.0,0.0,"glnA1 glnA Rv2220 MTCY190.31 MTCY427.01",null,"FUNCTION: Involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:7937767, PubMed:12819079). Also able to use GTP (PubMed:7937767). D-glutamate is a poor substrate, and DL-glutamate shows about 50% of the standard specific activity (PubMed:7937767). Also plays a key role in controlling the ammonia levels within infected host cells and so contributes to the pathogens capacity to inhibit phagosome acidification and phagosome-lysosome fusion (PubMed:7937767, PubMed:12819079). Involved in cell wall biosynthesis via the production of the major component poly-L-glutamine (PLG) (PubMed:7937767, PubMed:10618433). PLG synthesis in the cell wall occurs only in nitrogen limiting conditions and on the contrary high nitrogen conditions inhibit PLG synthesis (Probable). {ECO:0000269|PubMed:10618433, ECO:0000269|PubMed:12819079, ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:9278431}.","CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:19695264};","1HTO;1HTQ;2BVC;2WGS;2WHI;3ZXR;3ZXV;4ACF;4XYC;","DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[120.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","P9WIL5",100.0,0.0,"panC Rv3602c MTCY07H7B.20","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000269|PubMed:11669627}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000269|PubMed:12717031};","1MOP;1N2B;1N2E;1N2G;1N2H;1N2I;1N2J;1N2O;2A7X;2A84;2A86;2A88;3COV;3COW;3COY;3COZ;3IMC;3IME;3IMG;3IOB;3IOC;3IOD;3IOE;3ISJ;3IUB;3IUE;3IVC;3IVG;3IVX;3LE8;4DDH;4DDK;4DDM;4DE5;4EF6;4EFK;4FZJ;4G5F;4G5Y;","DB03107","Beta-Alanine","experimental","unknown"]
[121.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","P9WIL5",100.0,0.0,"panC Rv3602c MTCY07H7B.20","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000269|PubMed:11669627}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000269|PubMed:12717031};","1MOP;1N2B;1N2E;1N2G;1N2H;1N2I;1N2J;1N2O;2A7X;2A84;2A86;2A88;3COV;3COW;3COY;3COZ;3IMC;3IME;3IMG;3IOB;3IOC;3IOD;3IOE;3ISJ;3IUB;3IUE;3IVC;3IVG;3IVX;3LE8;4DDH;4DDK;4DDM;4DE5;4EF6;4EFK;4FZJ;4G5F;4G5Y;","DB02694","Pantoyl Adenylate","experimental","unknown"]
[122.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","P9WIL5",100.0,0.0,"panC Rv3602c MTCY07H7B.20","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000269|PubMed:11669627}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000269|PubMed:12717031};","1MOP;1N2B;1N2E;1N2G;1N2H;1N2I;1N2J;1N2O;2A7X;2A84;2A86;2A88;3COV;3COW;3COY;3COZ;3IMC;3IME;3IMG;3IOB;3IOC;3IOD;3IOE;3ISJ;3IUB;3IUE;3IVC;3IVG;3IVX;3LE8;4DDH;4DDK;4DDM;4DE5;4EF6;4EFK;4FZJ;4G5F;4G5Y;","DB01930","2,4-Dihydroxy-3,3-Dimethyl-Butyrate","experimental","unknown"]
[123.0,"6.3.2.1","Pantothenate synthetase","Mycobacterium tuberculosis","P9WIL5","BE0001387","P9WIL5",100.0,0.0,"panC Rv3602c MTCY07H7B.20","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000269|PubMed:11669627}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000269|PubMed:12717031};","1MOP;1N2B;1N2E;1N2G;1N2H;1N2I;1N2J;1N2O;2A7X;2A84;2A86;2A88;3COV;3COW;3COY;3COZ;3IMC;3IME;3IMG;3IOB;3IOC;3IOD;3IOE;3ISJ;3IUB;3IUE;3IVC;3IVG;3IVX;3LE8;4DDH;4DDK;4DDM;4DE5;4EF6;4EFK;4FZJ;4G5F;4G5Y;","DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]

{"sheet":"S. aureus FBA-only","index":16,"n_rows":76,"n_cols":19,"rows_kept":76,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.205","Inosine-5'-monophosphate dehydrogenase","Streptococcus pyogenes","P0C0H6","BE0002047","Q2G0Y7",66.8,0.0,"guaB SAOUHSC_00374","Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. ","FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. {ECO:0000255|HAMAP-Rule:MF_01964}.","CATALYTIC ACTIVITY: Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_01964};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[1.0,"1.1.1.205","Inosine-5'-monophosphate dehydrogenase","Streptococcus pyogenes","P0C0H6","BE0002047","Q2G0Y7",66.8,0.0,"guaB SAOUHSC_00374","Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. ","FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. {ECO:0000255|HAMAP-Rule:MF_01964}.","CATALYTIC ACTIVITY: Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_01964};",null,"DB04862","Merimepodib","investigational","unknown"]
[2.0,"1.1.1.88","3-hydroxy-3-methylglutaryl-coenzyme A reductase","Pseudomonas mevalonii","P13702","BE0001856","Q2FV77",40.1,7.599999999999998E-93,"SAOUHSC_02859","Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88; Evidence={ECO:0000256|RuleBase:RU361219};",null,"DB03785","(3r,5r)-7-((1r,2r,6s,8r,8as)-2,6-Dimethyl-8-{[(2r)-2-Methylbutanoyl]Oxy}-1,2,6,7,8,8a-Hexahydronaphthalen-1-Yl)-3,5-Dihydroxyheptanoic Acid","experimental","unknown"]
[3.0,"1.1.1.88","3-hydroxy-3-methylglutaryl-coenzyme A reductase","Pseudomonas mevalonii","P13702","BE0001856","Q2FV77",40.1,7.599999999999998E-93,"SAOUHSC_02859","Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88; Evidence={ECO:0000256|RuleBase:RU361219};",null,"DB03518","Mevalonic acid","experimental","unknown"]
[4.0,"1.1.1.88","3-hydroxy-3-methylglutaryl-coenzyme A reductase","Pseudomonas mevalonii","P13702","BE0001856","Q2FV77",40.1,7.599999999999998E-93,"SAOUHSC_02859","Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88; Evidence={ECO:0000256|RuleBase:RU361219};",null,"DB03169","(S)-Hmg-Coa","experimental","unknown"]
[5.0,"1.1.1.88","3-hydroxy-3-methylglutaryl-coenzyme A reductase","Pseudomonas mevalonii","P13702","BE0001856","Q2FV77",40.1,7.599999999999998E-93,"SAOUHSC_02859","Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88; Evidence={ECO:0000256|RuleBase:RU361219};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[6.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Staphylococcus aureus (strain MW2)","P61432","BE0002972","Q2G069",100.0,0.0,"murB SAOUHSC_00752","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[7.0,"1.3.3.4","Protoporphyrinogen oxidase","Bacillus subtilis (strain 168)","P32397","BE0003808","Q2FXA5",46.8,4.4999999999999995E-141,"SAOUHSC_01960","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1. ","FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. {ECO:0000256|RuleBase:RU364052}.","CATALYTIC ACTIVITY: Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX; Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4; Evidence={ECO:0000256|RuleBase:RU364052};",null,"DB07338","Acifluorfen","experimental","unknown"]
[8.0,"1.5.1.3","Dihydrofolate reductase","Bacillus anthracis","Q81R22","BE0004248","Q2FYK6",43.8,1.0999999999999999E-44,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[9.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB06847","5-[(3S)-3-(2-methoxybiphenyl-4-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[10.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[11.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07153","6-methyl-5-[3-methyl-3-(3,4,5-trimethoxyphenyl)but-1-yn-1-yl]pyrimidine-2,4-diamine","experimental","unknown"]
[12.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07142","5-[(3R)-3-(5-methoxy-3',5'-dimethylbiphenyl-3-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[13.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07140","5-[(3R)-3-(5-methoxybiphenyl-3-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[14.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","Q2FYK6",100.0,1.7999999999999997E-114,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07938","5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-chroman-5-yl]methyl]pyrimidine-2,4-diamine","experimental","unknown"]
[15.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","Q2FYK6",100.0,1.7999999999999997E-114,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[16.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","Q2FYK6",100.0,1.7999999999999997E-114,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB08741","5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-2H-chromen-5-yl]methyl]pyrimidine-2,4-diamine","experimental","unknown"]
[17.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","Q2FUZ8",36.7,2.3999999999999992E-132,"SAOUHSC_02947","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01115428};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[18.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","Q2FUZ8",36.7,2.3999999999999992E-132,"SAOUHSC_02947","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01115428};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[19.0,"2.2.1.1","Transketolase","Bacillus anthracis","Q81Y15","BE0004301","Q2FYT8",60.5,0.0,"SAOUHSC_01337",{"$nulls":4},"DB02078","Triglyme","experimental","unknown"]
[20.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q2FW49",46.5,3.999999999999999E-169,"SAOUHSC_02468",{"$nulls":4},"DB02327","Triethylene glycol","experimental","unknown"]
[21.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q2FW49",46.5,3.999999999999999E-169,"SAOUHSC_02468",{"$nulls":4},"DB03361","2-{(9as)-9a-[(1s)-1-Hydroxyethyl]-2,7-Dimethyl-9a,10-Dihydro-5h-Pyrimido[4,5-D][1,3]Thiazolo[3,2-a]Pyrimidin-8-Yl}Ethyl Trihydrogen Diphosphate","experimental","unknown"]
[22.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q2FW49",46.5,3.999999999999999E-169,"SAOUHSC_02468",{"$nulls":4},"DB01987","Cocarboxylase","approved, experimental","unknown"]
[23.0,"2.4.2.14","Amidophosphoribosyltransferase","Bacillus subtilis (strain 168)","P00497","BE0001375","Q2FZI9",56.2,0.0,"purF SAOUHSC_01014","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[24.0,"2.4.2.2","Pyrimidine-nucleoside phosphorylase","Geobacillus stearothermophilus","P77836","BE0003081","Q2FWC1",71.8,0.0,"pdp pyn SAOUHSC_02377",null,"FUNCTION: Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate. {ECO:0000250|UniProtKB:P77836}.","CATALYTIC ACTIVITY: Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.2; Evidence={ECO:0000250|UniProtKB:P77836}; CATALYTIC ACTIVITY: Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate + thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2; Evidence={ECO:0000250|UniProtKB:P77836}; CATALYTIC ACTIVITY: Reaction=2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + uracil; Xref=Rhea:RHEA:22824, ChEBI:CHEBI:16450, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2; Evidence={ECO:0000250|UniProtKB:P77836};",null,"DB03419","Uracil","experimental, investigational","unknown"]
[25.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Bacillus subtilis (strain 168)","P11998","BE0001767","Q2FXG2",67.3,5.299999999999999E-68,"ribH SAOUHSC_01886","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB04162","5-Nitro-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[26.0,"2.6.1.21","D-alanine aminotransferase","Bacillus sp. (strain YM-1)","P19938","BE0001509","Q2FXI0",52.0,2.899999999999999E-94,"SAOUHSC_01867",null,"FUNCTION: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. {ECO:0000256|RuleBase:RU004520}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + D-alanine = D-glutamate + pyruvate; Xref=Rhea:RHEA:15869, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810, ChEBI:CHEBI:29986, ChEBI:CHEBI:57416; EC=2.6.1.21; Evidence={ECO:0000256|RuleBase:RU004520};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[27.0,"2.7.4.3","Adenylate kinase","Bacillus subtilis (strain 168)","P16304","BE0001237","Q2FW27",68.4,3.099999999999999E-104,"adk SAOUHSC_02490","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|SAAS:SAAS01123758};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[28.0,"2.7.4.3","Adenylate kinase","Geobacillus stearothermophilus","P27142","BE0001254","Q2FW27",62.8,2.1999999999999996E-97,"adk SAOUHSC_02490","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|SAAS:SAAS01123758};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[29.0,"2.7.4.3","Adenylate kinase","Bacillus globisporus","P84139","BE0001255","Q2FW27",67.0,3.899999999999999E-100,"adk SAOUHSC_02490","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|SAAS:SAAS01123758};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[30.0,"2.7.6.1","Ribose-phosphate pyrophosphokinase","Bacillus subtilis (strain 168)","P14193","BE0001675","Q2G0S2",76.8,2.0999999999999992E-169,"prs SAOUHSC_00472","Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. ","FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). {ECO:0000256|HAMAP-Rule:MF_00583}.","CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000256|SAAS:SAAS01115190};",null,"DB02798","Alpha-Methylene Adenosine Monophosphate","experimental","unknown"]
[31.0,"2.7.6.1","Ribose-phosphate pyrophosphokinase","Bacillus subtilis (strain 168)","P14193","BE0001675","Q2G0S2",76.8,2.0999999999999992E-169,"prs SAOUHSC_00472","Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. ","FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). {ECO:0000256|HAMAP-Rule:MF_00583}.","CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000256|SAAS:SAAS01115190};",null,"DB03148","Phosphomethylphosphonic Acid Adenosyl Ester","experimental","unknown"]
[32.0,"2.7.7.23","Bifunctional protein GlmU","Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)","Q97R46","BE0003075","Q2G0S3",49.3,4.499999999999999E-147,"glmU SAOUHSC_00471","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[33.0,"2.7.7.39","Glycerol-3-phosphate cytidylyltransferase","Bacillus subtilis (strain 168)","P27623","BE0001644","Q2G2X2",69.5,1.4999999999999996E-63,"tarD SAOUHSC_00645","Cell wall biogenesis; poly(ribitol phosphate) teichoic acid biosynthesis. ","FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to sn-glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit by TarB and TarF. {ECO:0000269|PubMed:12637027}.","CATALYTIC ACTIVITY: Reaction=CTP + H(+) + sn-glycerol 3-phosphate = CDP-glycerol + diphosphate; Xref=Rhea:RHEA:13361, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57597, ChEBI:CHEBI:58311; EC=2.7.7.39; Evidence={ECO:0000269|PubMed:12637027};","2B7L;","DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[34.0,"2.7.7.39","Glycerol-3-phosphate cytidylyltransferase","Bacillus subtilis (strain 168)","P27623","BE0001644","Q2G2X2",69.5,1.4999999999999996E-63,"tarD SAOUHSC_00645","Cell wall biogenesis; poly(ribitol phosphate) teichoic acid biosynthesis. ","FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to sn-glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit by TarB and TarF. {ECO:0000269|PubMed:12637027}.","CATALYTIC ACTIVITY: Reaction=CTP + H(+) + sn-glycerol 3-phosphate = CDP-glycerol + diphosphate; Xref=Rhea:RHEA:13361, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57597, ChEBI:CHEBI:58311; EC=2.7.7.39; Evidence={ECO:0000269|PubMed:12637027};","2B7L;","DB02484","Cytidine 5'-Diphosphoglycerol","experimental","unknown"]
[35.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","Q9KPI8","BE0003891","Q2FXX8",53.9,2.0999999999999996E-75,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB07463","(3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(butylsulfanyl)methyl]pyrrolidin-3-ol","experimental","unknown"]
[36.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli O157:H7","P0AF14","BE0004031","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB07649","(3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(benzylsulfanyl)methyl]pyrrolidin-3-ol","experimental","unknown"]
[37.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB08606","(3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(METHYLSULFANYL)METHYL]PYRROLIDIN-3-OL","experimental","unknown"]
[38.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB02933","5'-Deoxy-5'-(Methylthio)-Tubercidin","experimental","unknown"]
[39.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB00173","Adenine","approved, nutraceutical","unknown"]
[40.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB02281","Formycin","experimental","unknown"]
[41.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB02158","(1s)-1-(9-Deazaadenin-9-Yl)-1,4,5-Trideoxy-1,4-Imino-5-Methylthio-D-Ribitol","experimental","unknown"]
[42.0,"3.5.4.5","Cytidine deaminase","Bacillus subtilis (strain 168)","P19079","BE0001980","Q2FY04",50.0,4.0E-35,"SAOUHSC_01670",null,"FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. {ECO:0000256|RuleBase:RU364006}.","CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+); Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5; Evidence={ECO:0000256|RuleBase:RU364006}; CATALYTIC ACTIVITY: Reaction=cytidine + H(+) + H2O = NH4(+) + uridine; Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5; Evidence={ECO:0000256|RuleBase:RU364006};",null,"DB03562","Tetrahydrodeoxyuridine","experimental","unknown"]
[43.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB01906","3-(5-Amino-7-Hydroxy-[1,2,3]Triazolo[4,5-D]Pyrimidin-2-Yl)-Benzoic Acid","experimental","unknown"]
[44.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB02119","6-Hydroxymethyl-7,8-Dihydropterin","experimental","unknown"]
[45.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB04168","2-Amino-5-Bromo-6-Phenylpyrimidin-4-Ol","experimental","unknown"]
[46.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB02489","9-Methylguanine","experimental","unknown"]
[47.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB01778","8-Amino-1,3-Dimethyl-3,7-Dihydropurine-2,6-Dione","experimental","unknown"]
[48.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB03571","3-(5-Amino-7-Hydroxy-[1,2,3]Triazolo[4,5-D]Pyrimidin-2-Yl)-N-(3,5-Dichlorobenzyl)-Benzamide","experimental","unknown"]
[49.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB04425","7,8-Dihydroneopterin","experimental","unknown"]
[50.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB03231","3-(5-Amino-7-oxo-3,7-dihydro-2H-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(2-{[2-(hydroxymethyl)phenyl]sulfanyl}benzyl)benzamide","experimental","unknown"]
[51.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB06906","2-AMINO-4-HYDROXYPYRIMIDINE-5-CARBOXYLIC ACID ETHYL ESTER","experimental","unknown"]
[52.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB04400","L-erythro-7,8-dihydrobiopterin","experimental","unknown"]
[53.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","Q2G002",97.9,2.1999999999999994E-165,"aroD SAOUHSC_00832","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[54.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","Q2G002",34.1,7.900000000000001E-29,"aroD SAOUHSC_00832","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[55.0,"4.2.3.4","3-dehydroquinate synthase","Staphylococcus aureus (strain MRSA252)","Q6GGU4","BE0001691","Q2FYH0",98.3,0.0,"aroB SAOUHSC_01482","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. ","FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-Rule:MF_00110}.","CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00110};",null,"DB02592","Carbaphosphonate","experimental","unknown"]
[56.0,"4.2.3.5","Chorismate synthase","Streptococcus pneumoniae (strain ATCC BAA-255 / R6)","P0A2Y7","BE0001922","Q2FYG9",56.6,4.199999999999999E-144,"aroC SAOUHSC_01483","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03350","Cobalt Hexammine Ion","experimental","unknown"]
[57.0,"4.2.3.5","Chorismate synthase","Streptococcus pneumoniae (strain ATCC BAA-255 / R6)","P0A2Y7","BE0001922","Q2FYG9",56.6,4.199999999999999E-144,"aroC SAOUHSC_01483","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[58.0,"4.99.1.1","Ferrochelatase","Bacillus subtilis (strain 168)","P32396","BE0001307","Q2FXA4",62.8,2.2999999999999993E-135,"hemH SAOUHSC_01961","Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. ","FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS00982002}.","CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS01116640};",null,"DB02188","N-Methylmesoporphyrin Containing Copper","experimental","unknown"]
[59.0,"4.99.1.1","Ferrochelatase","Bacillus subtilis (strain 168)","P32396","BE0001307","Q2FXA4",62.8,2.2999999999999993E-135,"hemH SAOUHSC_01961","Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. ","FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS00982002}.","CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS01116640};",null,"DB01911","N-Methylmesoporphyrin","experimental","unknown"]
[60.0,"5.1.1.3","Glutamate racemase","Helicobacter pylori (strain J99 / ATCC 700824)","Q9ZLT0","BE0004383","Q2FZC6",33.6,9.699999999999998E-36,"murI SAOUHSC_01106","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.","CATALYTIC ACTIVITY: Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813, ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00258};",null,"DB08698","1-[(3S)-5-PHENYL-3-THIOPHEN-2-YL-3H-1,4-BENZODIAZEPIN-2-YL]AZETIDIN-3-OL","experimental","unknown"]
[61.0,"5.1.1.3","Glutamate racemase","Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)","Q8Y7N7","BE0003797","Q2FZC6",50.9,2.0E-81,"murI SAOUHSC_01106","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.","CATALYTIC ACTIVITY: Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813, ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00258};",null,"DB02343","3,6,9,12,15-Pentaoxaheptadecane","experimental","unknown"]
[62.0,"5.1.1.3","Glutamate racemase","Streptococcus pyogenes serotype M1","Q9A1B7","BE0004263","Q2FZC6",43.7,3.2999999999999995E-69,"murI SAOUHSC_01106","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.","CATALYTIC ACTIVITY: Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813, ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00258};",null,"DB08272","(4S)-4-(2-NAPHTHYLMETHYL)-D-GLUTAMIC ACID","experimental","unknown"]
[63.0,"5.1.1.3","Glutamate racemase","Enterococcus faecalis (strain ATCC 700802 / V583)","Q836J0","BE0004137","Q2FZC6",50.8,2.0E-75,"murI SAOUHSC_01106","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.","CATALYTIC ACTIVITY: Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813, ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00258};",null,"DB07937","2-butoxy-9-(2,6-difluorobenzyl)-N-(2-morpholin-4-ylethyl)-9H-purin-6-amine","experimental","unknown"]
[64.0,"5.3.3.2","Isopentenyl-diphosphate delta-isomerase","Bacillus subtilis (strain 168)","P50740","BE0003039","Q2FVR9",41.6,2.0999999999999995E-83,"fni SAOUHSC_02623",null,"FUNCTION: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00354}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00354};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[65.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Bacillus subtilis (strain 168)","P08164","BE0001601","Q2G236",51.3,4.699999999999999E-83,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[66.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Bacillus subtilis (strain 168)","P08164","BE0001601","Q2G236",51.3,4.699999999999999E-83,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB04099","Deamido-Nad+","experimental","unknown"]
[67.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Bacillus subtilis (strain 168)","P08164","BE0001601","Q2G236",51.3,4.699999999999999E-83,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB00798","Gentamicin","approved, vet_approved","unknown"]
[68.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Escherichia coli (strain K12)","P18843","BE0001332","Q2G236",58.6,6.199999999999998E-104,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB02937","Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-Diphosphate","experimental","unknown"]
[69.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Escherichia coli (strain K12)","P18843","BE0001332","Q2G236",58.6,6.199999999999998E-104,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB04099","Deamido-Nad+","experimental","unknown"]
[70.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Escherichia coli (strain K12)","P18843","BE0001332","Q2G236",58.6,6.199999999999998E-104,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[71.0,"6.3.2.17","Folylpolyglutamate synthase","Lactobacillus casei","P15925","BE0001492","Q2FXR9",32.7,9.5E-62,"SAOUHSC_01766",{"$nulls":4},"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[72.0,"6.3.2.17","Folylpolyglutamate synthase","Lactobacillus casei","P15925","BE0001492","Q2FXR9",32.7,9.5E-62,"SAOUHSC_01766",{"$nulls":4},"DB03755","Adenosine-5'-[Beta, Gamma-Methylene]Tetraphosphate","experimental","unknown"]
[73.0,"6.3.2.17","Folylpolyglutamate synthase","Lactobacillus casei","P15925","BE0001492","Q2FXR9",32.7,9.5E-62,"SAOUHSC_01766",{"$nulls":4},"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]
[74.0,"6.3.2.17","Folylpolyglutamate synthase","Lactobacillus casei","P15925","BE0001492","Q2FXR9",32.7,9.5E-62,"SAOUHSC_01766",{"$nulls":4},"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]

{"sheet":"S. aureus FBA+FVA","index":17,"n_rows":67,"n_cols":19,"rows_kept":67,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.88","3-hydroxy-3-methylglutaryl-coenzyme A reductase","Pseudomonas mevalonii","P13702","BE0001856","Q2FV77",40.1,7.599999999999998E-93,"SAOUHSC_02859","Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88; Evidence={ECO:0000256|RuleBase:RU361219};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[1.0,"1.1.1.88","3-hydroxy-3-methylglutaryl-coenzyme A reductase","Pseudomonas mevalonii","P13702","BE0001856","Q2FV77",40.1,7.599999999999998E-93,"SAOUHSC_02859","Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88; Evidence={ECO:0000256|RuleBase:RU361219};",null,"DB03785","(3r,5r)-7-((1r,2r,6s,8r,8as)-2,6-Dimethyl-8-{[(2r)-2-Methylbutanoyl]Oxy}-1,2,6,7,8,8a-Hexahydronaphthalen-1-Yl)-3,5-Dihydroxyheptanoic Acid","experimental","unknown"]
[2.0,"1.1.1.88","3-hydroxy-3-methylglutaryl-coenzyme A reductase","Pseudomonas mevalonii","P13702","BE0001856","Q2FV77",40.1,7.599999999999998E-93,"SAOUHSC_02859","Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88; Evidence={ECO:0000256|RuleBase:RU361219};",null,"DB03518","Mevalonic acid","experimental","unknown"]
[3.0,"1.1.1.88","3-hydroxy-3-methylglutaryl-coenzyme A reductase","Pseudomonas mevalonii","P13702","BE0001856","Q2FV77",40.1,7.599999999999998E-93,"SAOUHSC_02859","Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88; Evidence={ECO:0000256|RuleBase:RU361219};",null,"DB03169","(S)-Hmg-Coa","experimental","unknown"]
[4.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Staphylococcus aureus (strain MW2)","P61432","BE0002972","Q2G069",100.0,0.0,"murB SAOUHSC_00752","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[5.0,"1.3.3.4","Protoporphyrinogen oxidase","Bacillus subtilis (strain 168)","P32397","BE0003808","Q2FXA5",46.8,4.4999999999999995E-141,"SAOUHSC_01960","Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1. ","FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. {ECO:0000256|RuleBase:RU364052}.","CATALYTIC ACTIVITY: Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX; Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4; Evidence={ECO:0000256|RuleBase:RU364052};",null,"DB07338","Acifluorfen","experimental","unknown"]
[6.0,"1.5.1.3","Dihydrofolate reductase","Bacillus anthracis","Q81R22","BE0004248","Q2FYK6",43.8,1.0999999999999999E-44,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[7.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","Q2FYK6",100.0,1.7999999999999997E-114,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07938","5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-chroman-5-yl]methyl]pyrimidine-2,4-diamine","experimental","unknown"]
[8.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","Q2FYK6",100.0,1.7999999999999997E-114,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[9.0,"1.5.1.3","Dihydrofolate reductase","Staphylococcus aureus","P0A017","BE0004138","Q2FYK6",100.0,1.7999999999999997E-114,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB08741","5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-2H-chromen-5-yl]methyl]pyrimidine-2,4-diamine","experimental","unknown"]
[10.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB06847","5-[(3S)-3-(2-methoxybiphenyl-4-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[11.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB08234","5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine","experimental","unknown"]
[12.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07153","6-methyl-5-[3-methyl-3-(3,4,5-trimethoxyphenyl)but-1-yn-1-yl]pyrimidine-2,4-diamine","experimental","unknown"]
[13.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07142","5-[(3R)-3-(5-methoxy-3',5'-dimethylbiphenyl-3-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[14.0,"1.5.1.3","Dihydrofolate reductase (dfrB)","Staphylococcus aureus (strain bovine RF122 / ET3-1)","A0A0M3KKX1","BE0009124","Q2FYK6",100.0,5.499999999999999E-113,"SAOUHSC_01434","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07140","5-[(3R)-3-(5-methoxybiphenyl-3-yl)but-1-yn-1-yl]-6-methylpyrimidine-2,4-diamine","experimental","unknown"]
[15.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","Q2FUZ8",36.7,2.3999999999999992E-132,"SAOUHSC_02947","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01115428};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[16.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","Q2FUZ8",36.7,2.3999999999999992E-132,"SAOUHSC_02947","Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. ","FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000256|SAAS:SAAS00040600}.","CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000256|SAAS:SAAS01115428};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[17.0,"2.2.1.1","Transketolase","Bacillus anthracis","Q81Y15","BE0004301","Q2FYT8",60.5,0.0,"SAOUHSC_01337",{"$nulls":4},"DB02078","Triglyme","experimental","unknown"]
[18.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q2FW49",46.5,3.999999999999999E-169,"SAOUHSC_02468",{"$nulls":4},"DB02327","Triethylene glycol","experimental","unknown"]
[19.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q2FW49",46.5,3.999999999999999E-169,"SAOUHSC_02468",{"$nulls":4},"DB03361","2-{(9as)-9a-[(1s)-1-Hydroxyethyl]-2,7-Dimethyl-9a,10-Dihydro-5h-Pyrimido[4,5-D][1,3]Thiazolo[3,2-a]Pyrimidin-8-Yl}Ethyl Trihydrogen Diphosphate","experimental","unknown"]
[20.0,"2.2.1.6","Acetolactate synthase, catabolic","Klebsiella pneumoniae","P27696","BE0001531","Q2FW49",46.5,3.999999999999999E-169,"SAOUHSC_02468",{"$nulls":4},"DB01987","Cocarboxylase","approved, experimental","unknown"]
[21.0,"2.4.2.14","Amidophosphoribosyltransferase","Bacillus subtilis (strain 168)","P00497","BE0001375","Q2FZI9",56.2,0.0,"purF SAOUHSC_01014","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[22.0,"2.4.2.2","Pyrimidine-nucleoside phosphorylase","Geobacillus stearothermophilus","P77836","BE0003081","Q2FWC1",71.8,0.0,"pdp pyn SAOUHSC_02377",null,"FUNCTION: Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate. {ECO:0000250|UniProtKB:P77836}.","CATALYTIC ACTIVITY: Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.2; Evidence={ECO:0000250|UniProtKB:P77836}; CATALYTIC ACTIVITY: Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate + thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2; Evidence={ECO:0000250|UniProtKB:P77836}; CATALYTIC ACTIVITY: Reaction=2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + uracil; Xref=Rhea:RHEA:22824, ChEBI:CHEBI:16450, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2; Evidence={ECO:0000250|UniProtKB:P77836};",null,"DB03419","Uracil","experimental, investigational","unknown"]
[23.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Bacillus subtilis (strain 168)","P11998","BE0001767","Q2FXG2",67.3,5.299999999999999E-68,"ribH SAOUHSC_01886","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB04162","5-Nitro-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[24.0,"2.7.4.3","Adenylate kinase","Geobacillus stearothermophilus","P27142","BE0001254","Q2FW27",62.8,2.1999999999999996E-97,"adk SAOUHSC_02490","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|SAAS:SAAS01123758};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[25.0,"2.7.4.3","Adenylate kinase","Bacillus globisporus","P84139","BE0001255","Q2FW27",67.0,3.899999999999999E-100,"adk SAOUHSC_02490","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|SAAS:SAAS01123758};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[26.0,"2.7.4.3","Adenylate kinase","Bacillus subtilis (strain 168)","P16304","BE0001237","Q2FW27",68.4,3.099999999999999E-104,"adk SAOUHSC_02490","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|SAAS:SAAS01123758};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[27.0,"2.7.6.1","Ribose-phosphate pyrophosphokinase","Bacillus subtilis (strain 168)","P14193","BE0001675","Q2G0S2",76.8,2.0999999999999992E-169,"prs SAOUHSC_00472","Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. ","FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). {ECO:0000256|HAMAP-Rule:MF_00583}.","CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000256|SAAS:SAAS01115190};",null,"DB02798","Alpha-Methylene Adenosine Monophosphate","experimental","unknown"]
[28.0,"2.7.6.1","Ribose-phosphate pyrophosphokinase","Bacillus subtilis (strain 168)","P14193","BE0001675","Q2G0S2",76.8,2.0999999999999992E-169,"prs SAOUHSC_00472","Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. ","FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). {ECO:0000256|HAMAP-Rule:MF_00583}.","CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000256|SAAS:SAAS01115190};",null,"DB03148","Phosphomethylphosphonic Acid Adenosyl Ester","experimental","unknown"]
[29.0,"2.7.7.39","Glycerol-3-phosphate cytidylyltransferase","Bacillus subtilis (strain 168)","P27623","BE0001644","Q2G2X2",69.5,1.4999999999999996E-63,"tarD SAOUHSC_00645","Cell wall biogenesis; poly(ribitol phosphate) teichoic acid biosynthesis. ","FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to sn-glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit by TarB and TarF. {ECO:0000269|PubMed:12637027}.","CATALYTIC ACTIVITY: Reaction=CTP + H(+) + sn-glycerol 3-phosphate = CDP-glycerol + diphosphate; Xref=Rhea:RHEA:13361, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57597, ChEBI:CHEBI:58311; EC=2.7.7.39; Evidence={ECO:0000269|PubMed:12637027};","2B7L;","DB02484","Cytidine 5'-Diphosphoglycerol","experimental","unknown"]
[30.0,"2.7.7.39","Glycerol-3-phosphate cytidylyltransferase","Bacillus subtilis (strain 168)","P27623","BE0001644","Q2G2X2",69.5,1.4999999999999996E-63,"tarD SAOUHSC_00645","Cell wall biogenesis; poly(ribitol phosphate) teichoic acid biosynthesis. ","FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to sn-glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit by TarB and TarF. {ECO:0000269|PubMed:12637027}.","CATALYTIC ACTIVITY: Reaction=CTP + H(+) + sn-glycerol 3-phosphate = CDP-glycerol + diphosphate; Xref=Rhea:RHEA:13361, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57597, ChEBI:CHEBI:58311; EC=2.7.7.39; Evidence={ECO:0000269|PubMed:12637027};","2B7L;","DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[31.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB08606","(3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(METHYLSULFANYL)METHYL]PYRROLIDIN-3-OL","experimental","unknown"]
[32.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB02933","5'-Deoxy-5'-(Methylthio)-Tubercidin","experimental","unknown"]
[33.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB00173","Adenine","approved, nutraceutical","unknown"]
[34.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB02158","(1s)-1-(9-Deazaadenin-9-Yl)-1,4,5-Trideoxy-1,4-Imino-5-Methylthio-D-Ribitol","experimental","unknown"]
[35.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli (strain K12)","P0AF12","BE0002007","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB02281","Formycin","experimental","unknown"]
[36.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Escherichia coli O157:H7","P0AF14","BE0004031","Q2FXX8",54.6,9.499999999999999E-77,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB07649","(3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(benzylsulfanyl)methyl]pyrrolidin-3-ol","experimental","unknown"]
[37.0,"3.2.2.9","5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","Q9KPI8","BE0003891","Q2FXX8",53.9,2.0999999999999996E-75,"mtnN SAOUHSC_01702","Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. ","FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.","CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};",null,"DB07463","(3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(butylsulfanyl)methyl]pyrrolidin-3-ol","experimental","unknown"]
[38.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB03571","3-(5-Amino-7-Hydroxy-[1,2,3]Triazolo[4,5-D]Pyrimidin-2-Yl)-N-(3,5-Dichlorobenzyl)-Benzamide","experimental","unknown"]
[39.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB02119","6-Hydroxymethyl-7,8-Dihydropterin","experimental","unknown"]
[40.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB01778","8-Amino-1,3-Dimethyl-3,7-Dihydropurine-2,6-Dione","experimental","unknown"]
[41.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB04400","L-erythro-7,8-dihydrobiopterin","experimental","unknown"]
[42.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB04425","7,8-Dihydroneopterin","experimental","unknown"]
[43.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB04168","2-Amino-5-Bromo-6-Phenylpyrimidin-4-Ol","experimental","unknown"]
[44.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB03231","3-(5-Amino-7-oxo-3,7-dihydro-2H-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(2-{[2-(hydroxymethyl)phenyl]sulfanyl}benzyl)benzamide","experimental","unknown"]
[45.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB02489","9-Methylguanine","experimental","unknown"]
[46.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB06906","2-AMINO-4-HYDROXYPYRIMIDINE-5-CARBOXYLIC ACID ETHYL ESTER","experimental","unknown"]
[47.0,"4.1.2.25","Dihydroneopterin aldolase","Staphylococcus aureus","P56740","BE0001289","Q2G0Q6",99.2,1.0999999999999997E-81,"SAOUHSC_00490","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. ","FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.","CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000256|RuleBase:RU362079};",null,"DB01906","3-(5-Amino-7-Hydroxy-[1,2,3]Triazolo[4,5-D]Pyrimidin-2-Yl)-Benzoic Acid","experimental","unknown"]
[48.0,"4.2.1.10","3-dehydroquinate dehydratase","Salmonella typhi","P24670","BE0001819","Q2G002",34.1,7.900000000000001E-29,"aroD SAOUHSC_00832","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00214};",null,"DB03746","3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate","experimental","unknown"]
[49.0,"4.2.1.10","3-dehydroquinate dehydratase","Staphylococcus aureus (strain MRSA252)","Q6GII7","BE0001690","Q2G002",97.9,2.1999999999999994E-165,"aroD SAOUHSC_00832","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. ","FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}.","CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00214};",null,"DB04347","3-Dehydroshikimate","experimental","unknown"]
[50.0,"4.2.3.4","3-dehydroquinate synthase","Staphylococcus aureus (strain MRSA252)","Q6GGU4","BE0001691","Q2FYH0",98.3,0.0,"aroB SAOUHSC_01482","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. ","FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-Rule:MF_00110}.","CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00110};",null,"DB02592","Carbaphosphonate","experimental","unknown"]
[51.0,"4.2.3.5","Chorismate synthase","Streptococcus pneumoniae (strain ATCC BAA-255 / R6)","P0A2Y7","BE0001922","Q2FYG9",56.6,4.199999999999999E-144,"aroC SAOUHSC_01483","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03350","Cobalt Hexammine Ion","experimental","unknown"]
[52.0,"4.2.3.5","Chorismate synthase","Streptococcus pneumoniae (strain ATCC BAA-255 / R6)","P0A2Y7","BE0001922","Q2FYG9",56.6,4.199999999999999E-144,"aroC SAOUHSC_01483","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[53.0,"4.99.1.1","Ferrochelatase","Bacillus subtilis (strain 168)","P32396","BE0001307","Q2FXA4",62.8,2.2999999999999993E-135,"hemH SAOUHSC_01961","Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. ","FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS00982002}.","CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS01116640};",null,"DB02188","N-Methylmesoporphyrin Containing Copper","experimental","unknown"]
[54.0,"4.99.1.1","Ferrochelatase","Bacillus subtilis (strain 168)","P32396","BE0001307","Q2FXA4",62.8,2.2999999999999993E-135,"hemH SAOUHSC_01961","Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. ","FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS00982002}.","CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS01116640};",null,"DB01911","N-Methylmesoporphyrin","experimental","unknown"]
[55.0,"5.3.3.2","Isopentenyl-diphosphate delta-isomerase","Bacillus subtilis (strain 168)","P50740","BE0003039","Q2FVR9",41.6,2.0999999999999995E-83,"fni SAOUHSC_02623",null,"FUNCTION: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00354}.","CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00354};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[56.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Escherichia coli (strain K12)","P18843","BE0001332","Q2G236",58.6,6.199999999999998E-104,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB02937","Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-Diphosphate","experimental","unknown"]
[57.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Escherichia coli (strain K12)","P18843","BE0001332","Q2G236",58.6,6.199999999999998E-104,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB04099","Deamido-Nad+","experimental","unknown"]
[58.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Escherichia coli (strain K12)","P18843","BE0001332","Q2G236",58.6,6.199999999999998E-104,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[59.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Bacillus subtilis (strain 168)","P08164","BE0001601","Q2G236",51.3,4.699999999999999E-83,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB02596","Alpha,Beta-Methyleneadenosine-5'-Triphosphate","experimental","unknown"]
[60.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Bacillus subtilis (strain 168)","P08164","BE0001601","Q2G236",51.3,4.699999999999999E-83,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB04099","Deamido-Nad+","experimental","unknown"]
[61.0,"6.3.1.5","NH(3)-dependent NAD(+) synthetase","Bacillus subtilis (strain 168)","P08164","BE0001601","Q2G236",51.3,4.699999999999999E-83,"nadE SAOUHSC_02132","Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. ","FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193}.","CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193};",null,"DB00798","Gentamicin","approved, vet_approved","unknown"]
[62.0,"6.3.2.17","Folylpolyglutamate synthase","Lactobacillus casei","P15925","BE0001492","Q2FXR9",32.7,9.5E-62,"SAOUHSC_01766",{"$nulls":4},"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[63.0,"6.3.2.17","Folylpolyglutamate synthase","Lactobacillus casei","P15925","BE0001492","Q2FXR9",32.7,9.5E-62,"SAOUHSC_01766",{"$nulls":4},"DB03755","Adenosine-5'-[Beta, Gamma-Methylene]Tetraphosphate","experimental","unknown"]
[64.0,"6.3.2.17","Folylpolyglutamate synthase","Lactobacillus casei","P15925","BE0001492","Q2FXR9",32.7,9.5E-62,"SAOUHSC_01766",{"$nulls":4},"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[65.0,"6.3.2.17","Folylpolyglutamate synthase","Lactobacillus casei","P15925","BE0001492","Q2FXR9",32.7,9.5E-62,"SAOUHSC_01766",{"$nulls":4},"DB02301","5,10-Methylene-6-Hydrofolic Acid","experimental","unknown"]

{"sheet":"P. putida FBA-only","index":18,"n_rows":300,"n_cols":19,"rows_kept":300,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.85","3-isopropylmalate dehydrogenase","Thiobacillus ferrooxidans","Q56268","BE0001699","Q88LE5",61.1,1.0999999999999998E-141,"leuB PP_1988","Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. ","FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. {ECO:0000255|HAMAP-Rule:MF_01033}.","CATALYTIC ACTIVITY: Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85; Evidence={ECO:0000255|HAMAP-Rule:MF_01033};",null,"DB04279","3-Isopropylmalic Acid","experimental","unknown"]
[1.0,"1.1.1.85","3-isopropylmalate dehydrogenase","Thiobacillus ferrooxidans","Q56268","BE0001699","L1LWW4",62.0,2.299999999999999E-141,"leuB CSV86_20174","Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. ","FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571560}.","CATALYTIC ACTIVITY: Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85; Evidence={ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS01118041};",null,"DB04279","3-Isopropylmalic Acid","experimental","unknown"]
[2.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","Q88DU4",65.5,1.1999999999999997E-116,"dapB PP_4725","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[3.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","Q88DU4",65.5,1.1999999999999997E-116,"dapB PP_4725","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[4.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","L1LV43",63.4,1.2999999999999997E-113,"dapB CSV86_22603","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[5.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","L1LV43",63.4,1.2999999999999997E-113,"dapB CSV86_22603","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[6.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","L1LTV6",45.5,1.7999999999999999E-78,"murB CSV86_26387","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS00057166}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|SAAS:SAAS01115694};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[7.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","L1LTV6",45.5,1.7999999999999999E-78,"murB CSV86_26387","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS00057166}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|SAAS:SAAS01115694};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[8.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q88LM5",43.7,1.1999999999999998E-80,"murB PP_1904","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[9.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q88LM5",43.7,1.1999999999999998E-80,"murB PP_1904","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[10.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone), mitochondrial","Plasmodium falciparum (isolate 3D7)","Q08210","BE0000612","Q88L40",37.1,4.5E-54,"pyrD PP_2095","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00225}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00225};",null,"DB01117","Atovaquone","approved","yes","inhibitor"]
[11.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone), mitochondrial","Plasmodium falciparum (isolate 3D7)","Q08210","BE0000612","L1LVM4",37.2,1.6E-56,"pyrD CSV86_23077","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS00750630}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS01124321};",null,"DB01117","Atovaquone","approved","yes","inhibitor"]
[12.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","L1LVM4",55.7,3.699999999999999E-125,"pyrD CSV86_23077","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS00750630}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS01124321};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[13.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","L1LVM4",55.7,3.699999999999999E-125,"pyrD CSV86_23077","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS00750630}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS01124321};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[14.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","L1LVM4",55.7,3.699999999999999E-125,"pyrD CSV86_23077","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS00750630}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS01124321};",null,"DB01942","Formic acid","experimental, investigational","unknown"]
[15.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","Q88L40",55.1,2.6999999999999996E-122,"pyrD PP_2095","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00225}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00225};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[16.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","Q88L40",55.1,2.6999999999999996E-122,"pyrD PP_2095","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00225}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00225};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[17.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","Q88L40",55.1,2.6999999999999996E-122,"pyrD PP_2095","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00225}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00225};",null,"DB01942","Formic acid","experimental, investigational","unknown"]
[18.0,"1.4.3.16","L-aspartate oxidase","Escherichia coli (strain K12)","P10902","BE0002969","L1M0H2",64.9,0.0,"CSV86_14219","Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1. ","FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate. {ECO:0000256|RuleBase:RU362049}.","CATALYTIC ACTIVITY: Reaction=L-aspartate + O2 = H2O2 + iminosuccinate; Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16; Evidence={ECO:0000256|RuleBase:RU362049};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[19.0,"1.4.3.16","L-aspartate oxidase","Escherichia coli (strain K12)","P10902","BE0002969","Q88MZ2",65.1,0.0,"nadB PP_1426","Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1. ","FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate. {ECO:0000256|RuleBase:RU362049}.","CATALYTIC ACTIVITY: Reaction=L-aspartate + O2 = H2O2 + iminosuccinate; Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16; Evidence={ECO:0000256|RuleBase:RU362049};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[20.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[21.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[22.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[23.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[24.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved, investigational","unknown"]
[25.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved, investigational","unknown"]
[26.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[27.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[28.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[29.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[30.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[31.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved, investigational","unknown"]
[32.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved, investigational","unknown"]
[33.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[34.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","Q88M71",41.1,2.1999999999999994E-121,"PP_1703",{"$nulls":4},"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[35.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","Q88M71",41.1,2.1999999999999994E-121,"PP_1703",{"$nulls":4},"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[36.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","L1LSB0",41.2,8.299999999999998E-119,"CSV86_27429",{"$nulls":4},"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[37.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","L1LSB0",41.2,8.299999999999998E-119,"CSV86_27429",{"$nulls":4},"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[38.0,"2.1.1.13","Methionine synthase","Escherichia coli (strain K12)","P13009","BE0001615","Q88KB5",66.5,0.0,"metH PP_2375","Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. ","FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. {ECO:0000256|PIRNR:PIRNR000381}.","CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13; Evidence={ECO:0000256|PIRNR:PIRNR000381};",null,"DB03614","Methylcobalamin","approved, experimental, investigational","unknown"]
[39.0,"2.1.1.13","Methionine synthase","Escherichia coli (strain K12)","P13009","BE0001615","L1LTM6",65.6,0.0,"metH CSV86_26662","Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. ","FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. {ECO:0000256|PIRNR:PIRNR000381}.","CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13; Evidence={ECO:0000256|PIRNR:PIRNR000381};",null,"DB03614","Methylcobalamin","approved, experimental, investigational","unknown"]
[40.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Neisseria meningitidis serogroup B (strain MC58)","Q9JZW6","BE0001822","Q88DW9",56.3,1.8999999999999995E-93,"panB PP_4699","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB04074","alpha-Ketoisovalerate","experimental","unknown"]
[41.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Neisseria meningitidis serogroup B (strain MC58)","Q9JZW6","BE0001822","L1LVP4",57.0,2.2999999999999994E-94,"panB CSV86_22738","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS00843518}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS01125081};",null,"DB04074","alpha-Ketoisovalerate","experimental","unknown"]
[42.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Escherichia coli (strain K12)","P31057","BE0001744","Q88DW9",56.8,3.199999999999999E-104,"panB PP_4699","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB03795","2-Dehydropantoate","experimental","unknown"]
[43.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Escherichia coli (strain K12)","P31057","BE0001744","L1LVP4",57.6,2.5999999999999995E-103,"panB CSV86_22738","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS00843518}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS01125081};",null,"DB03795","2-Dehydropantoate","experimental","unknown"]
[44.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","L1M648",42.0,2.0999999999999996E-56,"lpxA CSV86_03477","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[45.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","L1M648",42.0,2.0999999999999996E-56,"lpxA CSV86_03477","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[46.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","Q88MG8",38.7,3.3E-55,"lpxA PP_1603","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-Rule:MF_00387};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[47.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","Q88MG8",38.7,3.3E-55,"lpxA PP_1603","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-Rule:MF_00387};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[48.0,"2.3.3.9","Malate synthase G","Mycobacterium tuberculosis","P9WK17","BE0001750","L1LRV8",62.2,0.0,"glcB CSV86_28273","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[49.0,"2.3.3.9","Malate synthase G","Mycobacterium tuberculosis","P9WK17","BE0001750","L1LRV8",62.2,0.0,"glcB CSV86_28273","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB03499","Malate Ion","experimental","unknown"]
[50.0,"2.3.3.9","Malate synthase G","Mycobacterium tuberculosis","P9WK17","BE0001750","L1LRV8",62.2,0.0,"glcB CSV86_28273","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB04343","Glyoxylic acid","experimental","unknown"]
[51.0,"2.3.3.9","Malate synthase G","Mycobacterium tuberculosis","P9WK17","BE0001750","Q88QX8",67.2,0.0,"glcB PP_0356","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000255|HAMAP-Rule:MF_00641}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00641};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[52.0,"2.3.3.9","Malate synthase G","Mycobacterium tuberculosis","P9WK17","BE0001750","Q88QX8",67.2,0.0,"glcB PP_0356","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000255|HAMAP-Rule:MF_00641}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00641};",null,"DB03499","Malate Ion","experimental","unknown"]
[53.0,"2.3.3.9","Malate synthase G","Mycobacterium tuberculosis","P9WK17","BE0001750","Q88QX8",67.2,0.0,"glcB PP_0356","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000255|HAMAP-Rule:MF_00641}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00641};",null,"DB04343","Glyoxylic acid","experimental","unknown"]
[54.0,"2.3.3.9","Malate synthase G","Mycobacterium tuberculosis","P9WK17","BE0001750","L1LVV1",67.0,0.0,"glcB CSV86_22176","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[55.0,"2.3.3.9","Malate synthase G","Mycobacterium tuberculosis","P9WK17","BE0001750","L1LVV1",67.0,0.0,"glcB CSV86_22176","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB03499","Malate Ion","experimental","unknown"]
[56.0,"2.3.3.9","Malate synthase G","Mycobacterium tuberculosis","P9WK17","BE0001750","L1LVV1",67.0,0.0,"glcB CSV86_22176","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB04343","Glyoxylic acid","experimental","unknown"]
[57.0,"2.3.3.9","Malate synthase G","Escherichia coli (strain K12)","P37330","BE0001216","L1LRV8",65.7,0.0,"glcB CSV86_28273","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB04343","Glyoxylic acid","experimental","unknown"]
[58.0,"2.3.3.9","Malate synthase G","Escherichia coli (strain K12)","P37330","BE0001216","L1LRV8",65.7,0.0,"glcB CSV86_28273","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB01638","Sorbitol","approved","unknown"]
[59.0,"2.3.3.9","Malate synthase G","Escherichia coli (strain K12)","P37330","BE0001216","Q88QX8",60.0,0.0,"glcB PP_0356","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000255|HAMAP-Rule:MF_00641}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00641};",null,"DB04343","Glyoxylic acid","experimental","unknown"]
[60.0,"2.3.3.9","Malate synthase G","Escherichia coli (strain K12)","P37330","BE0001216","Q88QX8",60.0,0.0,"glcB PP_0356","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000255|HAMAP-Rule:MF_00641}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00641};",null,"DB01638","Sorbitol","approved","unknown"]
[61.0,"2.3.3.9","Malate synthase G","Escherichia coli (strain K12)","P37330","BE0001216","L1LVV1",58.1,0.0,"glcB CSV86_22176","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB04343","Glyoxylic acid","experimental","unknown"]
[62.0,"2.3.3.9","Malate synthase G","Escherichia coli (strain K12)","P37330","BE0001216","L1LVV1",58.1,0.0,"glcB CSV86_22176","Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. ","FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS01118129};",null,"DB01638","Sorbitol","approved","unknown"]
[63.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","L1M4R7",45.7,2.5999999999999996E-88,"murG CSV86_06901","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00765558}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS01124123};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[64.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","Q88C92",67.1,6.299999999999999E-100,"pyrE PP_5291","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[65.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","Q88C92",67.1,6.299999999999999E-100,"pyrE PP_5291","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB01632","5-O-phosphono-alpha-D-ribofuranosyl diphosphate","approved, experimental, investigational","unknown"]
[66.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","L1M443",66.7,2.5999999999999992E-99,"pyrE CSV86_07896","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[67.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","L1M443",66.7,2.5999999999999992E-99,"pyrE CSV86_07896","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB01632","5-O-phosphono-alpha-D-ribofuranosyl diphosphate","approved, experimental, investigational","unknown"]
[68.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","L1LWX6",64.2,0.0,"purF CSV86_20224","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[69.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","L1LWX6",64.2,0.0,"purF CSV86_20224","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[70.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","L1LWX6",64.2,0.0,"purF CSV86_20224","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[71.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q88LD5",63.8,0.0,"purF PP_2000","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[72.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q88LD5",63.8,0.0,"purF PP_2000","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[73.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q88LD5",63.8,0.0,"purF PP_2000","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[74.0,"2.4.2.19","Nicotinate-nucleotide pyrophosphorylase [carboxylating]","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P30012","BE0001347","L1LVL3",58.2,1.5999999999999996E-97,"CSV86_23012",{"$nulls":4},"DB01796","Quinolinic Acid","experimental","unknown"]
[75.0,"2.4.2.19","Nicotinate-nucleotide pyrophosphorylase [carboxylating]","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P30012","BE0001347","Q88PR1",59.3,3.3999999999999993E-99,"nadC PP_0787",{"$nulls":4},"DB01796","Quinolinic Acid","experimental","unknown"]
[76.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)","Q9S400","BE0001759","L1LSG3",49.1,5.499999999999999E-114,"aroA CSV86_27729","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00240586}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown","inhibitor"]
[77.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)","Q9S400","BE0001759","L1LSG3",49.1,5.499999999999999E-114,"aroA CSV86_27729","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00240586}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[78.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)","Q9S400","BE0001759","Q88M05",50.2,1.5999999999999998E-116,"aroA PP_1770","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00240586}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown","inhibitor"]
[79.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)","Q9S400","BE0001759","Q88M05",50.2,1.5999999999999998E-116,"aroA PP_1770","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00240586}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[80.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q88D60",72.4,0.0,"metK PP_4967","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[81.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q88D60",72.4,0.0,"metK PP_4967","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[82.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q88D60",72.4,0.0,"metK PP_4967","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[83.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","L1M122",72.6,0.0,"metK CSV86_12955","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000256|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[84.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","L1M122",72.6,0.0,"metK CSV86_12955","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000256|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[85.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","L1M122",72.6,0.0,"metK CSV86_12955","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000256|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[86.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[87.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[88.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[89.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[90.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[91.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[92.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[93.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[94.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[95.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[96.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q88P88",61.0,1.7999999999999994E-178,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[97.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","L1M2Q2",61.5,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[98.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q88P88",61.0,1.7999999999999994E-178,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[99.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","L1M2Q2",61.5,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[100.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Aquifex aeolicus (strain VF5)","O66529","BE0001449","Q88QH6",52.3,3.3E-51,"ribH PP_0517","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB02214","6,7-Dioxo-5h-8-Ribitylaminolumazine","experimental","unknown"]
[101.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Aquifex aeolicus (strain VF5)","O66529","BE0001449","Q88QH6",52.3,3.3E-51,"ribH PP_0517","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB04128","5-Nitroso-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[102.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Aquifex aeolicus (strain VF5)","O66529","BE0001449","Q88QH6",52.3,3.3E-51,"ribH PP_0517","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB04262","3-(7-hydroxy-8-ribityllumazine-6-yl) propionic acid","experimental","unknown"]
[103.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase 2","Brucella suis biovar 1 (strain 1330)","P61713","BE0001793","L1M2T7",30.3,1.0000000000000001E-11,"ribH CSV86_08813","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078298}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01115780};",null,"DB04162","5-Nitro-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[104.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase 2","Brucella suis biovar 1 (strain 1330)","P61713","BE0001793","Q88QH6",31.7,7.200000000000001E-12,"ribH PP_0517","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB04162","5-Nitro-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[105.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase 2","Brucella suis biovar 1 (strain 1330)","P61713","BE0001793","L1M0T2",62.6,6.8E-54,"ribH CSV86_12590","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078298}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01115780};",null,"DB04162","5-Nitro-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[106.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[107.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[108.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[109.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[110.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine hydroxamate","experimental","unknown"]
[111.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[112.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[113.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[114.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[115.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[116.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine hydroxamate","experimental","unknown"]
[117.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[118.0,"2.6.1.19","4-aminobutyrate aminotransferase GabT","Escherichia coli (strain K12)","P22256","BE0001510","L1LZQ5",73.9,0.0,"CSV86_14886",{"$nulls":4},"DB02783","4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate","experimental","unknown"]
[119.0,"2.6.1.19","4-aminobutyrate aminotransferase GabT","Escherichia coli (strain K12)","P22256","BE0001510","L1LZQ5",73.9,0.0,"CSV86_14886",{"$nulls":4},"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[120.0,"2.6.1.19","4-aminobutyrate aminotransferase GabT","Escherichia coli (strain K12)","P22256","BE0001510","Q88RB9",73.4,0.0,"davT PP_0214",null,"FUNCTION: Catalyzes the conversion of 5-aminovalerate to 5-oxopentanoate. {ECO:0000269|PubMed:11679348}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 5-aminopentanoate = 5-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:10212, ChEBI:CHEBI:16120, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:356010; EC=2.6.1.48; Evidence={ECO:0000269|PubMed:11679348};",null,"DB02783","4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate","experimental","unknown"]
[121.0,"2.6.1.19","4-aminobutyrate aminotransferase GabT","Escherichia coli (strain K12)","P22256","BE0001510","Q88RB9",73.4,0.0,"davT PP_0214",null,"FUNCTION: Catalyzes the conversion of 5-aminovalerate to 5-oxopentanoate. {ECO:0000269|PubMed:11679348}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 5-aminopentanoate = 5-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:10212, ChEBI:CHEBI:16120, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:356010; EC=2.6.1.48; Evidence={ECO:0000269|PubMed:11679348};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[122.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q88KG1",45.3,1.5999999999999998E-118,"pabB PP_2329",{"$nulls":4},"DB01942","Formic acid","experimental, investigational","unknown"]
[123.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","L1M7P7",46.4,3.7999999999999984E-120,"CSV86_01373",{"$nulls":4},"DB01942","Formic acid","experimental, investigational","unknown"]
[124.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X0D0","BE0001481","Q88P86",32.6,5.7E-40,"hisC PP_0967","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[125.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X0D0","BE0001481","Q88P86",32.6,5.7E-40,"hisC PP_0967","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB03997","L-histidinol phosphate","experimental","unknown"]
[126.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","Q88Q65",49.5,1.2E-58,"coaE PP_0631","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000255|HAMAP-Rule:MF_00376}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00376};",null,"DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[127.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","L1LW15",49.0,3.2999999999999996E-58,"coaE CSV86_20918","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000256|HAMAP-Rule:MF_00376}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24; Evidence={ECO:0000256|HAMAP-Rule:MF_00376};",null,"DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[128.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","L1LWK4",38.4,3.1E-41,"CSV86_21028","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[129.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","L1LWK4",38.4,3.1E-41,"CSV86_21028","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04345","Lumichrome","experimental","unknown"]
[130.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","L1LWK4",38.4,3.1E-41,"CSV86_21028","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[131.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q88Q93",37.7,7.9E-42,"ribF PP_0602","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[132.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q88Q93",37.7,7.9E-42,"ribF PP_0602","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04345","Lumichrome","experimental","unknown"]
[133.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q88Q93",37.7,7.9E-42,"ribF PP_0602","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[134.0,"2.7.2.8","Acetylglutamate kinase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HTN2","BE0001949","P59300",92.6,0.0,"argB PP_5289","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00082};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[135.0,"2.7.2.8","Acetylglutamate kinase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HTN2","BE0001949","L1M641",93.6,0.0,"argB CSV86_04857","Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. ","FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01159244}.","CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|SAAS:SAAS01124576};",null,"DB04075","N-Acetyl-L-Glutamate","experimental","unknown"]
[136.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","L1LTE5",64.8,1.8999999999999998E-87,"cmk CSV86_27734",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150952}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150969};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[137.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","L1LTE5",64.8,1.8999999999999998E-87,"cmk CSV86_27734",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150952}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150969};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[138.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","L1LTE5",64.8,1.8999999999999998E-87,"cmk CSV86_27734",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150952}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150969};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[139.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","L1LTE5",64.8,1.8999999999999998E-87,"cmk CSV86_27734",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150952}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150969};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[140.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q88M04",63.1,7.099999999999998E-85,"cmk PP_1771",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[141.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q88M04",63.1,7.099999999999998E-85,"cmk PP_1771",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[142.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q88M04",63.1,7.099999999999998E-85,"cmk PP_1771",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[143.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q88M04",63.1,7.099999999999998E-85,"cmk PP_1771",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[144.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","L1LWX9",66.8,1.1999999999999996E-91,"adk CSV86_20623","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS01123758};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[145.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","P0A136",64.1,3.999999999999999E-90,"adk PP_1506","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[146.0,"2.7.7.18","Nicotinate-nucleotide adenylyltransferase","Shigella flexneri","P0A753","BE0002611","L1M322",36.5,1.0E-36,"nadD CSV86_09817","Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. ","FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000256|HAMAP-Rule:MF_00244}.","CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18; Evidence={ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000256|SAAS:SAAS01124450};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[147.0,"2.7.7.18","Nicotinate-nucleotide adenylyltransferase","Shigella flexneri","P0A753","BE0002611","Q88DL5",35.6,5.099999999999999E-34,"nadD PP_4810","Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. ","FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000255|HAMAP-Rule:MF_00244}.","CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18; Evidence={ECO:0000255|HAMAP-Rule:MF_00244};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[148.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q88BX6",53.6,9.899999999999997E-167,"glmU PP_5411","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[149.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","L1LXA1",52.8,1.1999999999999996E-162,"glmU CSV86_19043","Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00381483}.","CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124206}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124218};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[150.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","L1M3V8",60.9,2.2E-60,"coaD CSV86_07136","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00395140}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069};",null,"DB03912","4'-Phosphopantetheine","experimental","unknown"]
[151.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","L1M3V8",60.9,2.2E-60,"coaD CSV86_07136","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00395140}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[152.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","L1M3V8",60.9,2.2E-60,"coaD CSV86_07136","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00395140}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069};",null,"DB03170","Dephospho Coenzyme A","experimental","unknown"]
[153.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q88CQ7",60.9,2.2999999999999998E-60,"coaD PP_5123","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};",null,"DB03912","4'-Phosphopantetheine","experimental","unknown"]
[154.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q88CQ7",60.9,2.2999999999999998E-60,"coaD PP_5123","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[155.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q88CQ7",60.9,2.2999999999999998E-60,"coaD PP_5123","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};",null,"DB03170","Dephospho Coenzyme A","experimental","unknown"]
[156.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","Q72K87","BE0001943","L1M3V8",53.3,8.0E-49,"coaD CSV86_07136","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00395140}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069};",null,"DB03912","4'-Phosphopantetheine","experimental","unknown"]
[157.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","Q72K87","BE0001943","Q88CQ7",53.3,1.0E-49,"coaD PP_5123","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};",null,"DB03912","4'-Phosphopantetheine","experimental","unknown"]
[158.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","Q88LM7",57.1,1.7999999999999999E-93,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[159.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","L1LTN0",54.4,9.899999999999999E-86,"kdsB CSV86_26397","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000256|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000256|HAMAP-Rule:MF_00057};",null,"DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[160.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[161.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[162.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[163.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[164.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB03721","N-acetyl-alpha-neuraminic acid","experimental","unknown"]
[165.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","L1M1X4",42.4,2.8E-37,"CSV86_10502",null,"FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[166.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","Q88P96",40.6,1.8999999999999998E-35,"kdsC PP_0956",null,"FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[167.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q88QF6",59.8,1.2999999999999997E-71,"ppa PP_0538",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};",null,"DB07291","5-amino-1-(4-chlorophenyl)-1H-pyrazole-4-carbonitrile","experimental","unknown"]
[168.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q88QF6",59.8,1.2999999999999997E-71,"ppa PP_0538",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};",null,"DB06851","N-(pyridin-3-ylmethyl)aniline","experimental","unknown"]
[169.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","L1M3J5",59.8,3.299999999999999E-72,"ppa CSV86_08703",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000256|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00209};",null,"DB07291","5-amino-1-(4-chlorophenyl)-1H-pyrazole-4-carbonitrile","experimental","unknown"]
[170.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","L1M3J5",59.8,3.299999999999999E-72,"ppa CSV86_08703",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000256|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00209};",null,"DB06851","N-(pyridin-3-ylmethyl)aniline","experimental","unknown"]
[171.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","L1M891",57.8,2.2999999999999997E-82,"pyrF CSV86_00296","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[172.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","L1M891",57.8,2.2999999999999997E-82,"pyrF CSV86_00296","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[173.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q88LW2",56.6,4.4E-82,"pyrF PP_1815","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-Rule:MF_01200}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[174.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q88LW2",56.6,4.4E-82,"pyrF PP_1815","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-Rule:MF_01200}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[175.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","L1LT51",35.0,1.1999999999999998E-39,"CSV86_26315",{"$nulls":4},"DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[176.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q88LL3",34.6,2.9999999999999995E-36,"pabC PP_1917",{"$nulls":4},"DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[177.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07732","2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[178.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07745","2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[179.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07748","2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[180.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07773","5-FLUOROINDOLE PROPANOL PHOSPHATE","experimental","unknown"]
[181.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07890","4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID","experimental","unknown"]
[182.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07894","4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[183.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07951","N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID","experimental","unknown"]
[184.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07952","N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID","experimental","unknown"]
[185.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07953","N-[1H-INDOL-3-YL-ACETYL]VALINE ACID","experimental","unknown"]
[186.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB04143","Indole-3-Glycerol Phosphate","experimental","unknown"]
[187.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[188.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07925","4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[189.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07745","2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[190.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07748","2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[191.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[192.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB04143","Indole-3-Glycerol Phosphate","experimental","unknown"]
[193.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07773","5-FLUOROINDOLE PROPANOL PHOSPHATE","experimental","unknown"]
[194.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07890","4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID","experimental","unknown"]
[195.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07894","4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[196.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07925","4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[197.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07732","2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[198.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07951","N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID","experimental","unknown"]
[199.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07952","N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID","experimental","unknown"]
[200.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07953","N-[1H-INDOL-3-YL-ACETYL]VALINE ACID","experimental","unknown"]
[201.0,"4.2.3.4","3-dehydroquinate synthase","Staphylococcus aureus (strain MRSA252)","Q6GGU4","BE0001691","Q88CV2",35.7,2.1E-53,"aroB PP_5078","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. ","FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-Rule:MF_00110}.","CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00110};",null,"DB02592","Carbaphosphonate","experimental","unknown"]
[202.0,"4.2.3.4","3-dehydroquinate synthase","Staphylococcus aureus (strain MRSA252)","Q6GGU4","BE0001691","L1M4I6",36.4,1.3999999999999998E-54,"aroB CSV86_07346","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. ","FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00858858}.","CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS01116881};",null,"DB02592","Carbaphosphonate","experimental","unknown"]
[203.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","Q88LU7",43.2,8.599999999999998E-96,"aroC PP_1830","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[204.0,"5.3.1.1","Triosephosphate isomerase","Vibrio marinus","P50921","BE0001889","L1LV54",47.2,7.299999999999999E-73,"tpiA CSV86_22653","Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. ","FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP-Rule:MF_00147}.","CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS01116239};",null,"DB02726","2-Phosphoglycolic Acid","experimental","unknown"]
[205.0,"5.3.1.1","Triosephosphate isomerase","Vibrio marinus","P50921","BE0001889","Q88DV4",49.2,2.5999999999999998E-73,"tpiA PP_4715","Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. ","FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.","CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};",null,"DB02726","2-Phosphoglycolic Acid","experimental","unknown"]
[206.0,"5.3.1.24","N-(5'-phosphoribosyl)anthranilate isomerase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q56320","BE0001549","L1LWX0",43.2,3.6999999999999997E-41,"trpF CSV86_20199","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. ",null,"CATALYTIC ACTIVITY: Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24; Evidence={ECO:0000256|HAMAP-Rule:MF_00135};",null,"DB03543","1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate","experimental","unknown"]
[207.0,"5.3.1.24","N-(5'-phosphoribosyl)anthranilate isomerase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q56320","BE0001549","Q88LE0",45.9,9.2E-42,"trpF PP_1995","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. ",null,"CATALYTIC ACTIVITY: Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00135};",null,"DB03543","1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate","experimental","unknown"]
[208.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","L1M4V0",90.8,5.999999999999999E-122,"gmhA CSV86_06836","Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. ","FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846114}.","CATALYTIC ACTIVITY: Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate; Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203, ChEBI:CHEBI:60204; EC=5.3.1.28; Evidence={ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS01116330};",null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[209.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","Q88N89",91.8,8.9E-124,"gmhA diaA PP_1323","Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. ","FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846114}.","CATALYTIC ACTIVITY: Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate; Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203, ChEBI:CHEBI:60204; EC=5.3.1.28; Evidence={ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS01116330};",null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[210.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","L1M3T3",58.6,1.1999999999999997E-82,"rpiA CSV86_06986","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00170, ECO:0000256|SAAS:SAAS00731113}.","CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00170, ECO:0000256|SAAS:SAAS01124525};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[211.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","Q88CN0",59.5,9.599999999999998E-80,"rpiA PP_5150","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[212.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","Q88CN0",62.9,2.0999999999999997E-88,"rpiA PP_5150","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};",null,"DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[213.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","L1M3T3",62.9,2.8999999999999996E-88,"rpiA CSV86_06986","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00170, ECO:0000256|SAAS:SAAS00731113}.","CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00170, ECO:0000256|SAAS:SAAS01124525};",null,"DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[214.0,"5.4.99.5","Secreted chorismate mutase","Mycobacterium tuberculosis","P9WIB9","BE0004361","L1M566",24.4,9.2E-6,"CSV86_05527",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[215.0,"6.3.2.1","Pantothenate synthetase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","Q5SHF5","BE0004567","Q88DW8",53.0,1.7E-82,"panC PP_4700","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03570","Tris-Hydroxymethyl-Methyl-Ammonium","experimental","unknown"]
[216.0,"6.3.2.1","Pantothenate synthetase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","Q5SHF5","BE0004567","L1LW46",51.4,1.5999999999999998E-77,"panC CSV86_22733","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000256|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00158, ECO:0000256|SAAS:SAAS01125062};",null,"DB03570","Tris-Hydroxymethyl-Methyl-Ammonium","experimental","unknown"]
[217.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","L1M4R1",46.4,3.0999999999999994E-129,"murE CSV86_06876","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[218.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","L1M4R1",46.4,3.0999999999999994E-129,"murE CSV86_06876","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[219.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","L1M4R1",46.4,3.0999999999999994E-129,"murE CSV86_06876","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[220.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q88N81",47.2,1.0999999999999997E-131,"murE PP_1332","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[221.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q88N81",47.2,1.0999999999999997E-131,"murE PP_1332","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[222.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q88N81",47.2,1.0999999999999997E-131,"murE PP_1332","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[223.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q88N75",57.8,0.0,"murC PP_1338","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[224.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q88N75",57.8,0.0,"murC PP_1338","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[225.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q88N75",57.8,0.0,"murC PP_1338","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[226.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","L1M4M7",58.0,0.0,"murC CSV86_06906","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[227.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","L1M4M7",58.0,0.0,"murC CSV86_06906","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[228.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","L1M4M7",58.0,0.0,"murC CSV86_06906","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[229.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[230.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[231.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[232.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[233.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[234.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[235.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[236.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[237.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[238.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[239.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[240.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[241.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[242.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[243.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[244.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[245.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[246.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[247.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[248.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[249.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[250.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[251.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[252.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[253.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[254.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[255.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[256.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[257.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[258.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[259.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[260.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[261.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[262.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[263.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[264.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[265.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[266.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[267.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","L1M1B0",69.3,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[268.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","L1M1B0",69.3,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[269.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","L1M1B0",69.3,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[270.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q88DD8",70.9,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[271.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q88DD8",70.9,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[272.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q88DD8",70.9,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[273.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","Q88DD8",70.7,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","Pentaglyme","experimental","unknown"]
[274.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","L1M1B0",69.3,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02580","Pentaglyme","experimental","unknown"]
[275.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[276.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[277.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[278.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[279.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[280.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[281.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[282.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[283.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02109","Hadacidin","experimental","unknown"]
[284.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[285.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[286.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[287.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[288.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[289.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[290.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[291.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[292.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[293.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","P59604",63.6,1.2999999999999997E-174,"argG PP_1088","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00005};",null,"DB02267","Argininosuccinate","experimental","unknown"]
[294.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","P59604",63.6,1.2999999999999997E-174,"argG PP_1088","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00005};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[295.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","L1M4C6",63.1,2.5999999999999993E-174,"argG CSV86_06591","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS01117911};",null,"DB02267","Argininosuccinate","experimental","unknown"]
[296.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","L1M4C6",63.1,2.5999999999999993E-174,"argG CSV86_06591","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS01117911};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[297.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","L1M2V6",71.2,0.0,"guaA CSV86_10832","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS00723675}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS01117722};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[298.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","Q88P21",70.7,0.0,"guaA PP_1032","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-Rule:MF_00344}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00344};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]

{"sheet":"P. putida FBA+FVA","index":19,"n_rows":283,"n_cols":19,"rows_kept":283,"cut":false,"hidden":false,"merged":[]}
[null,"EC NUMBER","PRODUCT","ORGANISM NAME","UNIPROTID","DRUGBANKID","HIT_UNIPROTID","PERCENT_IDENT_BLAST","EVALUE","GENE_NAME","PATHWAY","FUNCTION","CATALYTIC ACTIVITY","ID PDB","DRUGBANKDRUGID","DRUGNAME","DRUGGROUP","PHARMAACTION","ACTIONS"]
[0.0,"1.1.1.85","3-isopropylmalate dehydrogenase","Thiobacillus ferrooxidans","Q56268","BE0001699","L1LWW4",62.0,2.299999999999999E-141,"leuB CSV86_20174","Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. ","FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571560}.","CATALYTIC ACTIVITY: Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85; Evidence={ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS01118041};",null,"DB04279","3-Isopropylmalic Acid","experimental","unknown"]
[1.0,"1.1.1.85","3-isopropylmalate dehydrogenase","Thiobacillus ferrooxidans","Q56268","BE0001699","Q88LE5",61.1,1.0999999999999998E-141,"leuB PP_1988","Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. ","FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. {ECO:0000255|HAMAP-Rule:MF_01033}.","CATALYTIC ACTIVITY: Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85; Evidence={ECO:0000255|HAMAP-Rule:MF_01033};",null,"DB04279","3-Isopropylmalic Acid","experimental","unknown"]
[2.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","Q88DU4",65.5,1.1999999999999997E-116,"dapB PP_4725","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[3.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","Q88DU4",65.5,1.1999999999999997E-116,"dapB PP_4725","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[4.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","L1LV43",63.4,1.2999999999999997E-113,"dapB CSV86_22603","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB03363","3-Acetylpyridine Adenine Dinucleotide","experimental","unknown"]
[5.0,"1.17.1.8","4-hydroxy-tetrahydrodipicolinate reductase","Escherichia coli (strain K12)","P04036","BE0001986","L1LV43",63.4,1.2999999999999997E-113,"dapB CSV86_22603","Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. ","FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.","CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};",null,"DB04267","Dipicolinic Acid","experimental","unknown"]
[6.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","L1LTV6",45.5,1.7999999999999999E-78,"murB CSV86_26387","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS00057166}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|SAAS:SAAS01115694};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[7.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","L1LTV6",45.5,1.7999999999999999E-78,"murB CSV86_26387","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS00057166}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000256|SAAS:SAAS01115694};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[8.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q88LM5",43.7,1.1999999999999998E-80,"murB PP_1904","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[9.0,"1.3.1.98","UDP-N-acetylenolpyruvoylglucosamine reductase","Escherichia coli (strain K12)","P08373","BE0002971","Q88LM5",43.7,1.1999999999999998E-80,"murB PP_1904","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.","CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_00037};",null,"DB07296","(5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE","experimental","unknown"]
[10.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone), mitochondrial","Plasmodium falciparum (isolate 3D7)","Q08210","BE0000612","L1LVM4",37.2,1.6E-56,"pyrD CSV86_23077","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS00750630}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS01124321};",null,"DB01117","Atovaquone","approved","yes","inhibitor"]
[11.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone), mitochondrial","Plasmodium falciparum (isolate 3D7)","Q08210","BE0000612","Q88L40",37.1,4.5E-54,"pyrD PP_2095","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00225}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00225};",null,"DB01117","Atovaquone","approved","yes","inhibitor"]
[12.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","L1LVM4",55.7,3.699999999999999E-125,"pyrD CSV86_23077","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS00750630}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS01124321};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[13.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","L1LVM4",55.7,3.699999999999999E-125,"pyrD CSV86_23077","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS00750630}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS01124321};",null,"DB01942","Formic acid","experimental, investigational","unknown"]
[14.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","L1LVM4",55.7,3.699999999999999E-125,"pyrD CSV86_23077","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS00750630}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS01124321};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[15.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","Q88L40",55.1,2.6999999999999996E-122,"pyrD PP_2095","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00225}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00225};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[16.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","Q88L40",55.1,2.6999999999999996E-122,"pyrD PP_2095","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00225}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00225};",null,"DB01942","Formic acid","experimental, investigational","unknown"]
[17.0,"1.3.5.2","Dihydroorotate dehydrogenase (quinone)","Escherichia coli (strain K12)","P0A7E1","BE0001525","Q88L40",55.1,2.6999999999999996E-122,"pyrD PP_2095","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. ","FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00225}.","CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00225};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[18.0,"1.4.3.16","L-aspartate oxidase","Escherichia coli (strain K12)","P10902","BE0002969","L1M0H2",64.9,0.0,"CSV86_14219","Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1. ","FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate. {ECO:0000256|RuleBase:RU362049}.","CATALYTIC ACTIVITY: Reaction=L-aspartate + O2 = H2O2 + iminosuccinate; Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16; Evidence={ECO:0000256|RuleBase:RU362049};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[19.0,"1.4.3.16","L-aspartate oxidase","Escherichia coli (strain K12)","P10902","BE0002969","Q88MZ2",65.1,0.0,"nadB PP_1426","Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1. ","FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate. {ECO:0000256|RuleBase:RU362049}.","CATALYTIC ACTIVITY: Reaction=L-aspartate + O2 = H2O2 + iminosuccinate; Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16; Evidence={ECO:0000256|RuleBase:RU362049};",null,"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[20.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[21.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[22.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved, investigational","unknown"]
[23.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved, investigational","unknown"]
[24.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[25.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[26.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","L1M4I2",42.8,2.6000000000000002E-37,"CSV86_07056","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[27.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB12769","Lometrexol","investigational","unknown"]
[28.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02015","Dihydrofolic Acid","experimental","unknown"]
[29.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03904","Urea","approved, investigational","unknown"]
[30.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB11596","Levoleucovorin","approved, investigational","unknown"]
[31.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[32.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB07262","1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE","experimental","unknown"]
[33.0,"1.5.1.3","Dihydrofolate reductase","Escherichia coli (strain K12)","P0ABQ4","BE0002010","Q88CP8",42.8,1.4999999999999997E-36,"folA PP_5132","Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. ","FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.","CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000256|PIRNR:PIRNR000194};",null,"DB02363","2'-Monophosphoadenosine-5'-Diphosphate","experimental","unknown"]
[34.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","L1LSB0",41.2,8.299999999999998E-119,"CSV86_27429",{"$nulls":4},"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[35.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","L1LSB0",41.2,8.299999999999998E-119,"CSV86_27429",{"$nulls":4},"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[36.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","Q88M71",41.1,2.1999999999999994E-121,"PP_1703",{"$nulls":4},"DB03147","Flavin adenine dinucleotide","approved","unknown"]
[37.0,"1.8.1.2","Sulfite reductase [NADPH] flavoprotein alpha-component","Escherichia coli (strain K12)","P38038","BE0002963","Q88M71",41.1,2.1999999999999994E-121,"PP_1703",{"$nulls":4},"DB03461","2'-Monophosphoadenosine 5'-Diphosphoribose","experimental","unknown"]
[38.0,"2.1.1.13","Methionine synthase","Escherichia coli (strain K12)","P13009","BE0001615","Q88KB5",66.5,0.0,"metH PP_2375","Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. ","FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. {ECO:0000256|PIRNR:PIRNR000381}.","CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13; Evidence={ECO:0000256|PIRNR:PIRNR000381};",null,"DB03614","Methylcobalamin","approved, experimental, investigational","unknown"]
[39.0,"2.1.1.13","Methionine synthase","Escherichia coli (strain K12)","P13009","BE0001615","L1LTM6",65.6,0.0,"metH CSV86_26662","Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. ","FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. {ECO:0000256|PIRNR:PIRNR000381}.","CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13; Evidence={ECO:0000256|PIRNR:PIRNR000381};",null,"DB03614","Methylcobalamin","approved, experimental, investigational","unknown"]
[40.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Neisseria meningitidis serogroup B (strain MC58)","Q9JZW6","BE0001822","L1LVP4",57.0,2.2999999999999994E-94,"panB CSV86_22738","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS00843518}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS01125081};",null,"DB04074","alpha-Ketoisovalerate","experimental","unknown"]
[41.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Neisseria meningitidis serogroup B (strain MC58)","Q9JZW6","BE0001822","Q88DW9",56.3,1.8999999999999995E-93,"panB PP_4699","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB04074","alpha-Ketoisovalerate","experimental","unknown"]
[42.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Escherichia coli (strain K12)","P31057","BE0001744","Q88DW9",56.8,3.199999999999999E-104,"panB PP_4699","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-Rule:MF_00156}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00156};",null,"DB03795","2-Dehydropantoate","experimental","unknown"]
[43.0,"2.1.2.11","3-methyl-2-oxobutanoate hydroxymethyltransferase","Escherichia coli (strain K12)","P31057","BE0001744","L1LVP4",57.6,2.5999999999999995E-103,"panB CSV86_22738","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. ","FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS00843518}.","CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS01125081};",null,"DB03795","2-Dehydropantoate","experimental","unknown"]
[44.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","Q88MG8",38.7,3.3E-55,"lpxA PP_1603","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-Rule:MF_00387};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[45.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","Q88MG8",38.7,3.3E-55,"lpxA PP_1603","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-Rule:MF_00387};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[46.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","L1M648",42.0,2.0999999999999996E-56,"lpxA CSV86_03477","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB08558","2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL","experimental","unknown"]
[47.0,"2.3.1.129","Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase","Helicobacter pylori (strain ATCC 700392 / 26695)","O25927","BE0002505","L1M648",42.0,2.0999999999999996E-56,"lpxA CSV86_03477","Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. ","FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00943771}.","CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479, ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};",null,"DB01694","D-tartaric acid","experimental","unknown"]
[48.0,"2.4.1.227","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Escherichia coli (strain K12)","P17443","BE0001454","L1M4R7",45.7,2.5999999999999996E-88,"murG CSV86_06901","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00765558}.","CATALYTIC ACTIVITY: Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS01124123};",null,"DB02196","Uridine-Diphosphate-N-Acetylgalactosamine","experimental","unknown"]
[49.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","L1M443",66.7,2.5999999999999992E-99,"pyrE CSV86_07896","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB01632","5-O-phosphono-alpha-D-ribofuranosyl diphosphate","approved, experimental, investigational","unknown"]
[50.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","L1M443",66.7,2.5999999999999992E-99,"pyrE CSV86_07896","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[51.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","Q88C92",67.1,6.299999999999999E-100,"pyrE PP_5291","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB01632","5-O-phosphono-alpha-D-ribofuranosyl diphosphate","approved, experimental, investigational","unknown"]
[52.0,"2.4.2.10","Orotate phosphoribosyltransferase","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P08870","BE0001533","Q88C92",67.1,6.299999999999999E-100,"pyrE PP_5291","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. ","FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.","CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208};",null,"DB02262","Orotic Acid","experimental, investigational","unknown"]
[53.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q88LD5",63.8,0.0,"purF PP_2000","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[54.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q88LD5",63.8,0.0,"purF PP_2000","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[55.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","Q88LD5",63.8,0.0,"purF PP_2000","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[56.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","L1LWX6",64.2,0.0,"purF CSV86_20224","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB03942","Carboxylic PRPP","experimental","unknown"]
[57.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","L1LWX6",64.2,0.0,"purF CSV86_20224","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB01972","Guanosine-5'-Monophosphate","experimental","unknown"]
[58.0,"2.4.2.14","Amidophosphoribosyltransferase","Escherichia coli (strain K12)","P0AG16","BE0002042","L1LWX6",64.2,0.0,"purF CSV86_20224","Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. ","FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-Rule:MF_01931}.","CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};",null,"DB04296","5-Oxo-L-Norleucine","experimental","unknown"]
[59.0,"2.4.2.19","Nicotinate-nucleotide pyrophosphorylase [carboxylating]","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P30012","BE0001347","L1LVL3",58.2,1.5999999999999996E-97,"CSV86_23012",{"$nulls":4},"DB01796","Quinolinic Acid","experimental","unknown"]
[60.0,"2.4.2.19","Nicotinate-nucleotide pyrophosphorylase [carboxylating]","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P30012","BE0001347","Q88PR1",59.3,3.3999999999999993E-99,"nadC PP_0787",{"$nulls":4},"DB01796","Quinolinic Acid","experimental","unknown"]
[61.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)","Q9S400","BE0001759","Q88M05",50.2,1.5999999999999998E-116,"aroA PP_1770","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00240586}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown","inhibitor"]
[62.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)","Q9S400","BE0001759","Q88M05",50.2,1.5999999999999998E-116,"aroA PP_1770","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00240586}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[63.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)","Q9S400","BE0001759","L1LSG3",49.1,5.499999999999999E-114,"aroA CSV86_27729","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00240586}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04539","Glyphosate","experimental","unknown","inhibitor"]
[64.0,"2.5.1.19","3-phosphoshikimate 1-carboxyvinyltransferase","Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)","Q9S400","BE0001759","L1LSG3",49.1,5.499999999999999E-114,"aroA CSV86_27729","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. ","FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00240586}.","CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS01118199};",null,"DB04328","Shikimate-3-Phosphate","experimental","unknown"]
[65.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","L1M122",72.6,0.0,"metK CSV86_12955","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000256|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[66.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","L1M122",72.6,0.0,"metK CSV86_12955","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000256|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[67.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","L1M122",72.6,0.0,"metK CSV86_12955","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000256|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[68.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q88D60",72.4,0.0,"metK PP_4967","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[69.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q88D60",72.4,0.0,"metK PP_4967","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB03075","(Diphosphono)Aminophosphonic Acid","experimental","unknown"]
[70.0,"2.5.1.6","S-adenosylmethionine synthase","Shigella flexneri","P0A820","BE0001499","Q88D60",72.4,0.0,"metK PP_4967","Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. ","FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086};",null,"DB04554","8-Bromoadenosine-5'-Diphosphate","experimental","unknown"]
[71.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[72.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[73.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB02435","Aminomethylcyclohexane","experimental","unknown"]
[74.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[75.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","L1M2Q2",62.9,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[76.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB02995","Cyclohexylammonium Ion","experimental","unknown"]
[77.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB04174","3'-1-Carboxy-1-Phosphonooxy-Ethoxy-Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[78.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB02435","Aminomethylcyclohexane","experimental","unknown"]
[79.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB01879","(S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid","experimental","unknown"]
[80.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56)","P33038","BE0001291","Q88P88",62.7,0.0,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB04474","1-Anilino-8-Naphthalene Sulfonate","experimental","unknown"]
[81.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","Q88P88",61.0,1.7999999999999994E-178,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB00828","Fosfomycin","approved","yes","inhibitor"]
[82.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Escherichia coli (strain K12)","P0A749","BE0000468","L1M2Q2",61.5,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB00828","Fosfomycin","approved","yes","inhibitor"]
[83.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","Q88P88",61.0,1.7999999999999994E-178,"murA PP_0964","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111};","6CN1;","DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[84.0,"2.5.1.7","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Shigella flexneri","P0A751","BE0001252","L1M2Q2",61.5,0.0,"murA CSV86_10542","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767217}.","CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS01124343};",null,"DB03397","Uridine-Diphosphate-N-Acetylglucosamine","experimental","unknown"]
[85.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Aquifex aeolicus (strain VF5)","O66529","BE0001449","Q88QH6",52.3,3.3E-51,"ribH PP_0517","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB02214","6,7-Dioxo-5h-8-Ribitylaminolumazine","experimental","unknown"]
[86.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Aquifex aeolicus (strain VF5)","O66529","BE0001449","Q88QH6",52.3,3.3E-51,"ribH PP_0517","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB04262","3-(7-hydroxy-8-ribityllumazine-6-yl) propionic acid","experimental","unknown"]
[87.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase","Aquifex aeolicus (strain VF5)","O66529","BE0001449","Q88QH6",52.3,3.3E-51,"ribH PP_0517","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB04128","5-Nitroso-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[88.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase 2","Brucella suis biovar 1 (strain 1330)","P61713","BE0001793","L1M0T2",62.6,6.8E-54,"ribH CSV86_12590","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078298}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01115780};",null,"DB04162","5-Nitro-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[89.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase 2","Brucella suis biovar 1 (strain 1330)","P61713","BE0001793","Q88QH6",31.7,7.200000000000001E-12,"ribH PP_0517","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};",null,"DB04162","5-Nitro-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[90.0,"2.5.1.78","6,7-dimethyl-8-ribityllumazine synthase 2","Brucella suis biovar 1 (strain 1330)","P61713","BE0001793","L1M2T7",30.3,1.0000000000000001E-11,"ribH CSV86_08813","Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. ","FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078298}.","CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01115780};",null,"DB04162","5-Nitro-6-Ribityl-Amino-2,4(1h,3h)-Pyrimidinedione","experimental","unknown"]
[91.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[92.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[93.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine hydroxamate","experimental","unknown"]
[94.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[95.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[96.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","Q88BX8",63.0,0.0,"glmS PP_5409",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[97.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[98.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02445","2-Deoxy-2-Amino Glucitol-6-Phosphate","experimental","unknown"]
[99.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02446","Glutamine hydroxamate","experimental","unknown"]
[100.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02007","alpha-D-glucose 6-phosphate","experimental","unknown"]
[101.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB02657","Glucosamine 6-Phosphate","experimental","unknown"]
[102.0,"2.6.1.16","Glutamine--fructose-6-phosphate aminotransferase [isomerizing]","Escherichia coli (strain K12)","P17169","BE0001423","L1LXQ3",63.0,0.0,"glmS CSV86_19033",null,"FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.","CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00164};",null,"DB03581","Glucose-6-Phosphate","experimental","unknown"]
[103.0,"2.6.1.19","4-aminobutyrate aminotransferase GabT","Escherichia coli (strain K12)","P22256","BE0001510","Q88RB9",73.4,0.0,"davT PP_0214",null,"FUNCTION: Catalyzes the conversion of 5-aminovalerate to 5-oxopentanoate. {ECO:0000269|PubMed:11679348}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 5-aminopentanoate = 5-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:10212, ChEBI:CHEBI:16120, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:356010; EC=2.6.1.48; Evidence={ECO:0000269|PubMed:11679348};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[104.0,"2.6.1.19","4-aminobutyrate aminotransferase GabT","Escherichia coli (strain K12)","P22256","BE0001510","Q88RB9",73.4,0.0,"davT PP_0214",null,"FUNCTION: Catalyzes the conversion of 5-aminovalerate to 5-oxopentanoate. {ECO:0000269|PubMed:11679348}.","CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 5-aminopentanoate = 5-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:10212, ChEBI:CHEBI:16120, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:356010; EC=2.6.1.48; Evidence={ECO:0000269|PubMed:11679348};",null,"DB02783","4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate","experimental","unknown"]
[105.0,"2.6.1.19","4-aminobutyrate aminotransferase GabT","Escherichia coli (strain K12)","P22256","BE0001510","L1LZQ5",73.9,0.0,"CSV86_14886",{"$nulls":4},"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[106.0,"2.6.1.19","4-aminobutyrate aminotransferase GabT","Escherichia coli (strain K12)","P22256","BE0001510","L1LZQ5",73.9,0.0,"CSV86_14886",{"$nulls":4},"DB02783","4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate","experimental","unknown"]
[107.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","L1M7P7",46.4,3.7999999999999984E-120,"CSV86_01373",{"$nulls":4},"DB01942","Formic acid","experimental, investigational","unknown"]
[108.0,"2.6.1.85","Para-aminobenzoate synthase component 1","Escherichia coli (strain K12)","P05041","BE0000597","Q88KG1",45.3,1.5999999999999998E-118,"pabB PP_2329",{"$nulls":4},"DB01942","Formic acid","experimental, investigational","unknown"]
[109.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X0D0","BE0001481","Q88P86",32.6,5.7E-40,"hisC PP_0967","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB03997","L-histidinol phosphate","experimental","unknown"]
[110.0,"2.6.1.9","Histidinol-phosphate aminotransferase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9X0D0","BE0001481","Q88P86",32.6,5.7E-40,"hisC PP_0967","Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. ",null,"CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01023};",null,"DB02142","Pyridoxamine-5'-Phosphate","experimental","unknown"]
[111.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","L1LW15",49.0,3.2999999999999996E-58,"coaE CSV86_20918","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000256|HAMAP-Rule:MF_00376}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24; Evidence={ECO:0000256|HAMAP-Rule:MF_00376};",null,"DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[112.0,"2.7.1.24","Dephospho-CoA kinase","Escherichia coli (strain K12)","P0A6I9","BE0001231","Q88Q65",49.5,1.2E-58,"coaE PP_0631","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. ","FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. {ECO:0000255|HAMAP-Rule:MF_00376}.","CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; EC=2.7.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00376};",null,"DB01690","Bis(Adenosine)-5'-Triphosphate","experimental","unknown"]
[113.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q88Q93",37.7,7.9E-42,"ribF PP_0602","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04345","Lumichrome","experimental","unknown"]
[114.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q88Q93",37.7,7.9E-42,"ribF PP_0602","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[115.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","Q88Q93",37.7,7.9E-42,"ribF PP_0602","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[116.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","L1LWK4",38.4,3.1E-41,"CSV86_21028","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04345","Lumichrome","experimental","unknown"]
[117.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","L1LWK4",38.4,3.1E-41,"CSV86_21028","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[118.0,"2.7.1.26","Riboflavin biosynthesis protein RibF","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q9WZW1","BE0002551","L1LWK4",38.4,3.1E-41,"CSV86_21028","Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491}; CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[119.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q88M04",63.1,7.099999999999998E-85,"cmk PP_1771",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[120.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q88M04",63.1,7.099999999999998E-85,"cmk PP_1771",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[121.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q88M04",63.1,7.099999999999998E-85,"cmk PP_1771",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[122.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","Q88M04",63.1,7.099999999999998E-85,"cmk PP_1771",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00238};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[123.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","L1LTE5",64.8,1.8999999999999998E-87,"cmk CSV86_27734",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150952}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150969};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[124.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","L1LTE5",64.8,1.8999999999999998E-87,"cmk CSV86_27734",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150952}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150969};",null,"DB02883","2',3'-Dideoxycytidine-5'-Monophosphate","experimental","unknown"]
[125.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","L1LTE5",64.8,1.8999999999999998E-87,"cmk CSV86_27734",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150952}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150969};",null,"DB02456","Aracytidine 5'-monophosphate","experimental","unknown"]
[126.0,"2.7.4.25","Cytidylate kinase","Escherichia coli (strain K12)","P0A6I0","BE0001600","L1LTE5",64.8,1.8999999999999998E-87,"cmk CSV86_27734",null,null,"CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150952}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000256|SAAS:SAAS01150969};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[127.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","P0A136",64.1,3.999999999999999E-90,"adk PP_1506","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[128.0,"2.7.4.3","Adenylate kinase","Escherichia coli (strain K12)","P69441","BE0001244","L1LWX9",66.8,1.1999999999999996E-91,"adk CSV86_20623","Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. ","FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-Rule:MF_00235}.","CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS01123758};",null,"DB01717","Bis(Adenosine)-5'-Pentaphosphate","experimental","unknown"]
[129.0,"2.7.7.18","Nicotinate-nucleotide adenylyltransferase","Shigella flexneri","P0A753","BE0002611","Q88DL5",35.6,5.099999999999999E-34,"nadD PP_4810","Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. ","FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000255|HAMAP-Rule:MF_00244}.","CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18; Evidence={ECO:0000255|HAMAP-Rule:MF_00244};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[130.0,"2.7.7.18","Nicotinate-nucleotide adenylyltransferase","Shigella flexneri","P0A753","BE0002611","L1M322",36.5,1.0E-36,"nadD CSV86_09817","Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. ","FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000256|HAMAP-Rule:MF_00244}.","CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18; Evidence={ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000256|SAAS:SAAS01124450};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[131.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","Q88BX6",53.6,9.899999999999997E-167,"glmU PP_5411","Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.","CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[132.0,"2.7.7.23","Bifunctional protein GlmU","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P43889","BE0004280","L1LXA1",52.8,1.1999999999999996E-162,"glmU CSV86_19043","Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. ","FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00381483}.","CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124206}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS01124218};",null,"DB08344","4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide","experimental","unknown"]
[133.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","Q72K87","BE0001943","Q88CQ7",53.3,1.0E-49,"coaD PP_5123","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};",null,"DB03912","4'-Phosphopantetheine","experimental","unknown"]
[134.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","Q72K87","BE0001943","L1M3V8",53.3,8.0E-49,"coaD CSV86_07136","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00395140}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069};",null,"DB03912","4'-Phosphopantetheine","experimental","unknown"]
[135.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","L1M3V8",60.9,2.2E-60,"coaD CSV86_07136","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00395140}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069};",null,"DB03912","4'-Phosphopantetheine","experimental","unknown"]
[136.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","L1M3V8",60.9,2.2E-60,"coaD CSV86_07136","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00395140}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069};",null,"DB03170","Dephospho Coenzyme A","experimental","unknown"]
[137.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","L1M3V8",60.9,2.2E-60,"coaD CSV86_07136","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00395140}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[138.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q88CQ7",60.9,2.2999999999999998E-60,"coaD PP_5123","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};",null,"DB03912","4'-Phosphopantetheine","experimental","unknown"]
[139.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q88CQ7",60.9,2.2999999999999998E-60,"coaD PP_5123","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};",null,"DB03170","Dephospho Coenzyme A","experimental","unknown"]
[140.0,"2.7.7.3","Phosphopantetheine adenylyltransferase","Shigella flexneri","P0A6I8","BE0001757","Q88CQ7",60.9,2.2999999999999998E-60,"coaD PP_5123","Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. ","FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.","CATALYTIC ACTIVITY: Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151};",null,"DB01992","Coenzyme A","investigational, nutraceutical","unknown"]
[141.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[142.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB03403","Cytidine-5'-Monophosphate","experimental","unknown"]
[143.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB02431","Cytidine-5'-Triphosphate","experimental","unknown"]
[144.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB03721","N-acetyl-alpha-neuraminic acid","experimental","unknown"]
[145.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Escherichia coli","P42216","BE0001522","Q88LM7",45.3,4.7E-53,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB04555","Cytidine-5'-Diphosphate","experimental","unknown"]
[146.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","Q88LM7",57.1,1.7999999999999999E-93,"kdsB PP_1902","Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00057};",null,"DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[147.0,"2.7.7.38","3-deoxy-manno-octulosonate cytidylyltransferase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44490","BE0001714","L1LTN0",54.4,9.899999999999999E-86,"kdsB CSV86_26397","Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. ","FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000256|HAMAP-Rule:MF_00057}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000256|HAMAP-Rule:MF_00057};",null,"DB04482","Cmp-2-Keto-3-Deoxy-Octulosonic Acid","experimental","unknown"]
[148.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","L1M1X4",42.4,2.8E-37,"CSV86_10502",null,"FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[149.0,"3.1.3.45","3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45314","BE0003190","Q88P96",40.6,1.8999999999999998E-35,"kdsC PP_0956",null,"FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.","CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000256|PIRNR:PIRNR006118};",null,"DB03814","2-(N-Morpholino)-Ethanesulfonic Acid","experimental","unknown"]
[150.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q88QF6",59.8,1.2999999999999997E-71,"ppa PP_0538",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};",null,"DB07291","5-amino-1-(4-chlorophenyl)-1H-pyrazole-4-carbonitrile","experimental","unknown"]
[151.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","Q88QF6",59.8,1.2999999999999997E-71,"ppa PP_0538",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209};",null,"DB06851","N-(pyridin-3-ylmethyl)aniline","experimental","unknown"]
[152.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","L1M3J5",59.8,3.299999999999999E-72,"ppa CSV86_08703",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000256|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00209};",null,"DB07291","5-amino-1-(4-chlorophenyl)-1H-pyrazole-4-carbonitrile","experimental","unknown"]
[153.0,"3.6.1.1","Inorganic pyrophosphatase","Burkholderia pseudomallei (strain 1710b)","Q3JUV5","BE0003737","L1M3J5",59.8,3.299999999999999E-72,"ppa CSV86_08703",null,"FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000256|HAMAP-Rule:MF_00209}.","CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00209};",null,"DB06851","N-(pyridin-3-ylmethyl)aniline","experimental","unknown"]
[154.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","L1M891",57.8,2.2999999999999997E-82,"pyrF CSV86_00296","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[155.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","L1M891",57.8,2.2999999999999997E-82,"pyrF CSV86_00296","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[156.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q88LW2",56.6,4.4E-82,"pyrF PP_1815","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-Rule:MF_01200}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB02890","6-Hydroxyuridine-5'-Phosphate","experimental","unknown"]
[157.0,"4.1.1.23","Orotidine 5'-phosphate decarboxylase","Escherichia coli (strain K12)","P08244","BE0001677","Q88LW2",56.6,4.4E-82,"pyrF PP_1815","Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. ","FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-Rule:MF_01200}.","CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01200};",null,"DB03668","1-(5'-Phospho-Beta-D-Ribofuranosyl)Barbituric Acid","experimental","unknown"]
[158.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","Q88LL3",34.6,2.9999999999999995E-36,"pabC PP_1917",{"$nulls":4},"DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[159.0,"4.1.3.38","Aminodeoxychorismate lyase","Escherichia coli (strain K12)","P28305","BE0003132","L1LT51",35.0,1.1999999999999998E-39,"CSV86_26315",{"$nulls":4},"DB02038","D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide","experimental","unknown"]
[160.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07732","2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[161.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07745","2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[162.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07748","2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[163.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07773","5-FLUOROINDOLE PROPANOL PHOSPHATE","experimental","unknown"]
[164.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07890","4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID","experimental","unknown"]
[165.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07894","4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[166.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07925","4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[167.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07951","N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID","experimental","unknown"]
[168.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07953","N-[1H-INDOL-3-YL-ACETYL]VALINE ACID","experimental","unknown"]
[169.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB04143","Indole-3-Glycerol Phosphate","experimental","unknown"]
[170.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[171.0,"4.2.1.20","Tryptophan synthase alpha chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P00929","BE0004065","L1LYR0",38.4,3.5E-48,"trpA CSV86_18022","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111173}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01126077};",null,"DB07952","N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID","experimental","unknown"]
[172.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07732","2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[173.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07745","2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[174.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07953","N-[1H-INDOL-3-YL-ACETYL]VALINE ACID","experimental","unknown"]
[175.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07952","N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID","experimental","unknown"]
[176.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07951","N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID","experimental","unknown"]
[177.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07925","4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[178.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07894","4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID","experimental","unknown"]
[179.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07890","4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID","experimental","unknown"]
[180.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07773","5-FLUOROINDOLE PROPANOL PHOSPHATE","experimental","unknown"]
[181.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB07748","2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE","experimental","unknown"]
[182.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB04143","Indole-3-Glycerol Phosphate","experimental","unknown"]
[183.0,"4.2.1.20","Tryptophan synthase beta chain","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","P0A2K1","BE0004066","L1LXU8",56.2,1.3999999999999997E-151,"trpB CSV86_18017","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. ","FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.","CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS01118361};",null,"DB03171","Indole-3-Propanol Phosphate","experimental","unknown"]
[184.0,"4.2.3.4","3-dehydroquinate synthase","Staphylococcus aureus (strain MRSA252)","Q6GGU4","BE0001691","Q88CV2",35.7,2.1E-53,"aroB PP_5078","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. ","FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-Rule:MF_00110}.","CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00110};",null,"DB02592","Carbaphosphonate","experimental","unknown"]
[185.0,"4.2.3.4","3-dehydroquinate synthase","Staphylococcus aureus (strain MRSA252)","Q6GGU4","BE0001691","L1M4I6",36.4,1.3999999999999998E-54,"aroB CSV86_07346","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. ","FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00858858}.","CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS01116881};",null,"DB02592","Carbaphosphonate","experimental","unknown"]
[186.0,"4.2.3.5","Chorismate synthase","Helicobacter pylori (strain ATCC 700392 / 26695)","P56122","BE0003020","Q88LU7",43.2,8.599999999999998E-96,"aroC PP_1830","Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. ","FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.","CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300};",null,"DB03247","Flavin mononucleotide","approved, investigational","unknown"]
[187.0,"5.3.1.1","Triosephosphate isomerase","Vibrio marinus","P50921","BE0001889","Q88DV4",49.2,2.5999999999999998E-73,"tpiA PP_4715","Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. ","FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147}.","CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};",null,"DB02726","2-Phosphoglycolic Acid","experimental","unknown"]
[188.0,"5.3.1.1","Triosephosphate isomerase","Vibrio marinus","P50921","BE0001889","L1LV54",47.2,7.299999999999999E-73,"tpiA CSV86_22653","Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. ","FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP-Rule:MF_00147}.","CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS01116239};",null,"DB02726","2-Phosphoglycolic Acid","experimental","unknown"]
[189.0,"5.3.1.24","N-(5'-phosphoribosyl)anthranilate isomerase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q56320","BE0001549","L1LWX0",43.2,3.6999999999999997E-41,"trpF CSV86_20199","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. ",null,"CATALYTIC ACTIVITY: Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24; Evidence={ECO:0000256|HAMAP-Rule:MF_00135};",null,"DB03543","1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate","experimental","unknown"]
[190.0,"5.3.1.24","N-(5'-phosphoribosyl)anthranilate isomerase","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","Q56320","BE0001549","Q88LE0",45.9,9.2E-42,"trpF PP_1995","Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. ",null,"CATALYTIC ACTIVITY: Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00135};",null,"DB03543","1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate","experimental","unknown"]
[191.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","Q88N89",91.8,8.9E-124,"gmhA diaA PP_1323","Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. ","FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846114}.","CATALYTIC ACTIVITY: Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate; Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203, ChEBI:CHEBI:60204; EC=5.3.1.28; Evidence={ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS01116330};",null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[192.0,"5.3.1.28","Phosphoheptose isomerase","Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)","Q9HVZ0","BE0001887","L1M4V0",90.8,5.999999999999999E-122,"gmhA CSV86_06836","Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. ","FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846114}.","CATALYTIC ACTIVITY: Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate; Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203, ChEBI:CHEBI:60204; EC=5.3.1.28; Evidence={ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS01116330};",null,"DB02470","D-Glycero-D-Mannopyranose-7-Phosphate","experimental","unknown"]
[193.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","L1M3T3",62.9,2.8999999999999996E-88,"rpiA CSV86_06986","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00170, ECO:0000256|SAAS:SAAS00731113}.","CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00170, ECO:0000256|SAAS:SAAS01124525};",null,"DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[194.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Shigella flexneri","P0A7Z3","BE0001628","Q88CN0",62.9,2.0999999999999997E-88,"rpiA PP_5150","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};",null,"DB04127","beta-D-arabinofuranose 5-phosphate","experimental","unknown"]
[195.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","L1M3T3",58.6,1.1999999999999997E-82,"rpiA CSV86_06986","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00170, ECO:0000256|SAAS:SAAS00731113}.","CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00170, ECO:0000256|SAAS:SAAS01124525};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[196.0,"5.3.1.6","Ribose-5-phosphate isomerase A","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P44725","BE0003268","Q88CN0",59.5,9.599999999999998E-80,"rpiA PP_5150","Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. ","FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.","CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[197.0,"5.4.99.5","Secreted chorismate mutase","Mycobacterium tuberculosis","P9WIB9","BE0004361","L1M566",24.4,9.2E-6,"CSV86_05527",{"$nulls":4},"DB08648","(1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid","experimental","unknown"]
[198.0,"6.3.2.1","Pantothenate synthetase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","Q5SHF5","BE0004567","Q88DW8",53.0,1.7E-82,"panC PP_4700","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000255|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00158};",null,"DB03570","Tris-Hydroxymethyl-Methyl-Ammonium","experimental","unknown"]
[199.0,"6.3.2.1","Pantothenate synthetase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","Q5SHF5","BE0004567","L1LW46",51.4,1.5999999999999998E-77,"panC CSV86_22733","Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. ","FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000256|HAMAP-Rule:MF_00158}.","CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00158, ECO:0000256|SAAS:SAAS01125062};",null,"DB03570","Tris-Hydroxymethyl-Methyl-Ammonium","experimental","unknown"]
[200.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","L1M4R1",46.4,3.0999999999999994E-129,"murE CSV86_06876","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[201.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","L1M4R1",46.4,3.0999999999999994E-129,"murE CSV86_06876","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[202.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","L1M4R1",46.4,3.0999999999999994E-129,"murE CSV86_06876","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[203.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q88N81",47.2,1.0999999999999997E-131,"murE PP_1332","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[204.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q88N81",47.2,1.0999999999999997E-131,"murE PP_1332","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03590","2,6-Diaminopimelic Acid","experimental","unknown"]
[205.0,"6.3.2.13","UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase","Escherichia coli (strain K12)","P22188","BE0001538","Q88N81",47.2,1.0999999999999997E-131,"murE PP_1332","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00208}.","CATALYTIC ACTIVITY: Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[206.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","L1M4M7",58.0,0.0,"murC CSV86_06906","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[207.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","L1M4M7",58.0,0.0,"murC CSV86_06906","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[208.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","L1M4M7",58.0,0.0,"murC CSV86_06906","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01090476}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|SAAS:SAAS01124320};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[209.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q88N75",57.8,0.0,"murC PP_1338","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB03909","Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate","experimental","unknown"]
[210.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q88N75",57.8,0.0,"murC PP_1338","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[211.0,"6.3.2.8","UDP-N-acetylmuramate--L-alanine ligase","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","P45066","BE0001247","Q88N75",57.8,0.0,"murC PP_1338","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.","CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00046};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[212.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[213.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[214.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[215.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[216.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[217.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[218.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[219.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","Q88N78",49.7,2.8999999999999994E-124,"murD PP_1335","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000255|HAMAP-Rule:MF_00639}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00639};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[220.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08107","N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID","experimental","unknown"]
[221.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08112","N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[222.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08105","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid","experimental","unknown"]
[223.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB01673","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine","experimental","unknown"]
[224.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB02314","Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate","experimental","unknown"]
[225.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08108","N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID","experimental","unknown"]
[226.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB08106","N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid","experimental","unknown"]
[227.0,"6.3.2.9","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Escherichia coli (strain K12)","P14900","BE0001258","L1M458",51.4,3.599999999999999E-127,"murD CSV86_06891","Cell wall biogenesis; peptidoglycan biosynthesis. ","FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178092}.","CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178088};",null,"DB03801","Lysine Nz-Carboxylic Acid","experimental","unknown"]
[228.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[229.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[230.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[231.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[232.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[233.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[234.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[235.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[236.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[237.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[238.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","Q88QD6",70.5,0.0,"accC PP_0558","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[239.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08145","6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE","experimental","unknown"]
[240.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08075","4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine","experimental","unknown"]
[241.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08076","4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine","experimental","unknown"]
[242.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08144","6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine","experimental","unknown"]
[243.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08146","7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine","experimental","unknown"]
[244.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08314","(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE","experimental","unknown"]
[245.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08315","2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE","experimental","unknown"]
[246.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08316","4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one","experimental","unknown"]
[247.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08317","5-methyl-6-phenylquinazoline-2,4-diamine","experimental","unknown"]
[248.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08318","6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine","experimental","unknown"]
[249.0,"6.3.4.14","Biotin carboxylase","Escherichia coli (strain K12)","P24182","BE0004154","L1M243",70.3,0.0,"CSV86_11620","Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. ","FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000256|RuleBase:RU365063}.","CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000256|RuleBase:RU365063}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000256|RuleBase:RU365063};",null,"DB08074","3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine","experimental","unknown"]
[250.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[251.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[252.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[253.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02109","Hadacidin","experimental","unknown"]
[254.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[255.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[256.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[257.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[258.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","L1M1B0",69.5,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[259.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[260.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04460","(C8-S)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[261.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB03146","2-deazo-6-thiophosphate guanosine-5'-monophosphate","experimental","unknown"]
[262.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02109","Hadacidin","experimental","unknown"]
[263.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02493","Hydantocidin-5'-Phosphate","experimental","unknown"]
[264.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02666","(C8-R)-Hydantocidin 5'-Phosphate","experimental","unknown"]
[265.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04315","Guanosine-5'-Diphosphate","experimental","unknown"]
[266.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02836","Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate","experimental","unknown"]
[267.0,"6.3.4.4","Adenylosuccinate synthetase","Escherichia coli (strain K12)","P0A7D4","BE0001441","Q88DD8",71.2,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[268.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","L1M1B0",69.3,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[269.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","L1M1B0",69.3,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[270.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","L1M1B0",69.3,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[271.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q88DD8",70.9,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04566","Inosinic Acid","experimental","unknown"]
[272.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q88DD8",70.9,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02954","(Carboxyhydroxyamino)Ethanoic Acid","experimental","unknown"]
[273.0,"6.3.4.4","Adenylosuccinate synthetase","Shigella flexneri","Q83P33","BE0001828","Q88DD8",70.9,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB04160","Pyrophosphoric acid","approved, experimental","unknown"]
[274.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","L1M1B0",69.3,0.0,"purA CSV86_13380","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};",null,"DB02580","Pentaglyme","experimental","unknown"]
[275.0,"6.3.4.4","Adenylosuccinate synthetase","Yersinia pestis","Q8ZIV7","BE0004308","Q88DD8",70.7,0.0,"purA PP_4889","Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. ","FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.","CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00011};",null,"DB02580","Pentaglyme","experimental","unknown"]
[276.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","L1M4C6",63.1,2.5999999999999993E-174,"argG CSV86_06591","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS01117911};",null,"DB02267","Argininosuccinate","experimental","unknown"]
[277.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","L1M4C6",63.1,2.5999999999999993E-174,"argG CSV86_06591","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS01117911};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[278.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","P59604",63.6,1.2999999999999997E-174,"argG PP_1088","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00005};",null,"DB02267","Argininosuccinate","experimental","unknown"]
[279.0,"6.3.4.5","Argininosuccinate synthase","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","P59846","BE0001471","P59604",63.6,1.2999999999999997E-174,"argG PP_1088","Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. ",null,"CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00005};",null,"DB04395","Phosphoaminophosphonic Acid-Adenylate Ester","experimental","unknown"]
[280.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","Q88P21",70.7,0.0,"guaA PP_1032","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-Rule:MF_00344}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00344};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]
[281.0,"6.3.5.2","GMP synthase [glutamine-hydrolyzing]","Escherichia coli (strain K12)","P04079","BE0002545","L1M2V6",71.2,0.0,"guaA CSV86_10832","Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. ","FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS00723675}.","CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS01117722};",null,"DB04272","Citric Acid","approved, nutraceutical, vet_approved","unknown"]