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. Author manuscript; available in PMC: 2012 Jun 16.
Published in final edited form as: J Am Chem Soc. 2010 Dec 16;133(2):379–386. doi: 10.1021/ja107424t

Table 1.

Hypothetical functions of proteins adjacent to the thiocarboxylate-forming protein, HcyS-Ala.

Protein IDs Putative function of the proteins
WS1004, NP_907206 (sir) Ferredoxin sulfite reductase*
WS1005, NP_907207 (hcyD) Metalloprotease involved in the removal of C-terminal alanine of HcyS-Ala prior to sulfur transfer and also in the release of homocysteine from HcyS-Homocysteine adduct*
WS1006, NP_907208 (hcyF) ATP-utilizing enzyme involved in adenylating HcyS C-terminal prior to sulfur transfer*
WS1007, NP_907209 (hcyS-ala) Sulfur transfer protein involved in methionine biosynthesis*
WS1008 and WS1009, NP_907210 and NP_907211 (cysD and cysN) Sulfate adenylyltransferase, subunits 1 and 2
WS1010, NP_907212 (cysH) Phosphoadenylyl-sulfate reductase/Adenylyl-sulfate reductase
WS1011, NP_907213 Conserved hypothetical protein probably involved in assimilatory sulfate reduction
WS1012, NP_907214 (metY) O-acetylhomoserine sulfhydrylase*
WS1013, NP_907215 Methyltransferase (EC 2.1.1.-)
WS1014, NP_907216 Putative efflux protein
WS1015, NP_907217 (metZ) O-acetylhomoserine or O-succinylhomoserine sulfhydrylase*
*

Experimentally characterized in this study.