Table 1. Description of the 38 domains with a flavodoxin fold used as a dataset.
Protein | Origin | PDB | Res | Chain | Domain |
---|---|---|---|---|---|
Glutamate mutase | Clostridium tetanomorphum | 1BE1 | NMR | A | 00(1–137) |
B-12-binding domains of methionine synthase | Escherichia coli | 1BMT | 3 | A | 02(738–895) |
D-2-hydroxyisocaproate dehydrogenase | Lactobacillus casei | 1DXY | 1.86 | A | 02(102–297) |
CheY (signal transduction protein) | Escherichia coli | 1EAY | 2 | A | 00(2–129) |
Serine esterase | Streptomyces scabiei | 1ESD | 2.3 | A | 00(4–305) |
GTP-specific succynil-CoA synthetase | Sus scrofa | 1EUC | 2.1 | A | 01(9–131) |
Sus scrofa | 1EUC | 2.1 | A | 02(132–301) | |
Sus scrofa | 1EUC | 2.1 | B | 03(247–392) | |
Nucleoside 2-deoxyribosyl transferase | Lactobacillus leichmannii | 1F8Y | 2.4 | A | 00(2–157) |
Apo flavodoxin | Nostoc sp | 1FTG | 2 | A | 00(2–169) |
Platelet-activating factor acetylhydrolase IB | Bos taurus | 1FXW | 2.1 | A | 00(5–215) |
Bos taurus | 1FXW | 2.1 | F | 00(6–217) | |
Tir domain of human TLR1 | Homo sapiens | 1FYV | 2.9 | A | 00(625–785) |
NAD-dependent D-glycerate dehydrogenase | Hyphomicrobium methylovorum | 1GDH | 2.4 | A | 02(102–285) |
Type II dehydroquinase | Bacillus subtilis | 1GQO | 2.1 | A | 00(1–141) |
Type II dehydroquinase | Streptomyces coelicolor | 1GTZ | 1.6 | A | 00(2–150) |
Precorrin-8X methylmutase | Pseudomonas denitrificans | 1I1H | 2.6 | A | 00(2–210) |
D-lactase dehydrogenase | Lactobacillus delbrueckii subsp bulgaricus | 1J4A | 1.9 | A | 02(104–299) |
Succinyl-CoA synthetase | Escherichia coli | 1JKJ | 2.35 | A | 01(1–122) |
Escherichia coli | 1JKJ | 2.35 | A | 02(123–287) | |
Lysophospholiase L1/acyl-CoA thioesterase I/proteaseI | Escherichia coli | 1JRL | 1.95 | A | 00(1–179) |
S-adenosylhomocysteine hydrolase | Homo sapiens | 1LI4 | 2.01 | A | 02(193–352) |
CtBP dehydrogenase | Homo sapiens | 1MX3 | 1.95 | A | 02(125–318) |
Phosphoribosylalinoimidazole mutase | Thermotoga maritima | 1O4V | 1.77 | A | 00(2–170) |
Succinyl-CoA synthetase | Thermus thermophilus | 1OI7 | 1.23 | A | 01(1–122) |
PurE (lyase) | Escherichia coli | 1QCZ | 1.5 | A | 00(7–169) |
L-alanine dehydrogenase | Phormidium lapideum | 1SAY | 2.1 | A | 02(129–304) |
PurE (N5-carboxyaminoimidazole ribonucleotide mutase) | Acetobacter aceti | 1U11 | 1.55 | A | 00(20–178) |
Type II 3-dehydroquinate dehydratase | Actinobacillus pleuropneumoniae | 1UQR | 1.7 | A | 00(1–146) |
S-adenosyl-I-homocysteine hydrolase | Plasmodium falciparum | 1V8B | 2.4 | A | 02(237–397) |
PurE (lyase) | Bacillus anthracis | 1XMP | 1.8 | A | 00(2–156) |
D-3-phosphoglycerate dehydrogenase | Mycobacterium tuberculosis | 1YGY | 2.3 | A | 02(99–280) |
Lipase / acylhydrolase | Enterococcus faecalis | 1YZF | 1.9 | A | 00(1–195) |
GDSL-like lipase | Nostoc sp. PCC 7120 | 1Z8H | 2.02 | A | 00(5–206) |
Acetylxylan esterase | Clostridium acetobutylicum | 1ZMB | 2.61 | A | 01(2–248) |
Product of gene AT4G34215 | Arabidopsis thaliana | 2APJ | 1.6 | A | 00(17–260) |
H.pylori type II dehydroquinase | Helictobacter pylori | 2C4V | 2.5 | A | 00(1–158) |
Methylmalonyl-CoA mutase | Propionibacterium freudenreichii subsp. shermanii | 7REQ | 2.2 | A | 02(563–726) |
Res is the resolution in ångström for X-Ray structures, otherwise they provide from NMR. Limits in domain column are retrieved from CATH. Proteins are sorted according to their PDB code.