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nuoA nuoA glk glk talA talA tktB tktB hyfA hyfA hyfB hyfB hyfC hyfC hyfD hyfD hyfE hyfE hyfF hyfF hyfG hyfG hyfH hyfH hyfI hyfI fdx fdx yfjG yfjG norV norV hydN hydN hycG hycG hycF hycF hycE hycE hycD hycD hycC hycC hycB hycB ygcQ ygcQ ygcR ygcR ygcG ygcG ppc ppc gldA gldA tpiA tpiA pfkA pfkA fdoG fdoG talB talB fixA fixA fixB fixB aceE aceE aceF aceF lpd lpd acnB acnB cyoA cyoA cyoB cyoB cyoC cyoC cyoD cyoD frmA frmA prpD prpD fdoH fdoH fdoI fdoI hemG hemG ubiE ubiE eno eno yqcA yqcA ygfS ygfS fldB fldB rpiA rpiA fbaA fbaA pgk pgk tktA tktA glcB glcB hybC hybC yahG yahG prpC prpC lsrF lsrF dsbB dsbB icd-2 icd-2 ycfZ ycfZ yceJ yceJ torA torA hybB hybB hybA hybA hybO hybO mdh mdh rpe rpe glgA glgA glgC glgC glgX glgX glgB glgB yhjA yhjA bisC bisC yiaI yiaI gpmI gpmI aceB aceB aceA aceA aceK aceK pgi pgi nrfA nrfA nrfB nrfB nrfC nrfC alsE alsE fumB fumB dipZ dipZ aspA aspA yjeK yjeK frdC frdC frdB frdB frdA frdA CAR20769.1 CAR20769.1 cybC cybC nrdG nrdG hgdC hgdC ytjC ytjC fumC fumC fumA fumA rsxA rsxA rsxB rsxB rsxC rsxC rsxD rsxD rsxG rsxG rsxE rsxE ydhU ydhU ydhV ydhV ydhY ydhY pntB pntB pykF pykF ydiF ydiF ydiQ ydiQ ydiR ydiR gapA gapA zwf zwf pykA pykA torZ torZ torY torY yedZ yedZ gnd gnd fbaB fbaB dld dld grxA grxA ybhJ ybhJ pgl pgl gpmA gpmA cydB cydB cydA cydA glmS-2 glmS-2 glmE glmE CAR16834.1 CAR16834.1 sucD sucD sucC sucC sucB sucB yahF yahF ykgE ykgE fdrA fdrA ylbE ylbE ybdH ybdH fldA fldA gltA gltA sdhC sdhC sdhD sdhD sdhA sdhA sdhB sdhB sucA sucA ynfH ynfH ynfG ynfG ynfF ynfF ynfE ynfE acnA acnA ydbK ydbK ldhA ldhA azoR azoR fdnG fdnG fdnH fdnH fdnI fdnI torC torC torT torT appB appB appC appC hyaC hyaC hyaB hyaB hyaA hyaA dmsC dmsC dmsB dmsB dmsA dmsA yeiB yeiB napC napC napB napB napG napG napA napA mqo mqo yfaE yfaE glpC glpC nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoC nuoC nuoB nuoB
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proteins of unknown 3D structure
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nuoANADH:ubiquinone oxidoreductase, membrane subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. (147 aa)
glkGlucokinase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the bacterial glucokinase family. (321 aa)
talATransaldolase A; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (316 aa)
tktBTransketolase 2, thiamin-binding; 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. (667 aa)
hyfAHydrogenase 4, 4Fe-4S subunit; Function experimentally demonstrated in the studied species; carrier. (205 aa)
hyfBHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (672 aa)
hyfCHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (315 aa)
hyfDHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (479 aa)
hyfEHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (216 aa)
hyfFHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (526 aa)
hyfGHydrogenase 4, subunit; Function experimentally demonstrated in the studied species; carrier. (555 aa)
hyfHHydrogenase 4, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (181 aa)
hyfIHydrogenase 4, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (252 aa)
fdx[2Fe-2S] ferredoxin; Function experimentally demonstrated in the studied species; carrier. (111 aa)
yfjGConserved hypothetical protein; Homologs of previously reported genes of unknown function. (158 aa)
norVFlavorubredoxin oxidoreductase; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family. (479 aa)
hydNFormate dehydrogenase-H, [4Fe-4S] ferredoxin subunit; Function experimentally demonstrated in the studied species; carrier. (175 aa)
hycGHydrogenase 3 and formate hydrogenase complex, HycG subunit; Function experimentally demonstrated in the studied species; enzyme. (255 aa)
hycFFormate hydrogenlyase complex iron-sulfur protein; Function experimentally demonstrated in the studied species; carrier. (180 aa)
hycEHydrogenase 3, large subunit; Function experimentally demonstrated in the studied species; enzyme. (569 aa)
hycDHydrogenase 3, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (307 aa)
hycCHydrogenase 3, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (608 aa)
hycBHydrogenase 3, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (203 aa)
ygcQPutative flavoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (286 aa)
ygcRPutative flavoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (259 aa)
ygcGConserved hypothetical protein; Homologs of previously reported genes of unknown function. (290 aa)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. (883 aa)
gldAGlycerol dehydrogenase, NAD; Function experimentally demonstrated in the studied species; enzyme. (367 aa)
tpiATriosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (255 aa)
pfkA6-phosphofructokinase I; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. (320 aa)
fdoGFormate dehydrogenase-O, large subunit; Function experimentally demonstrated in the studied genus; enzyme. (1016 aa)
talBTransaldolase B; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (317 aa)
fixAPutative electron transfer flavoprotein subunit, ETFP adenine nucleotide-binding domain; Required for anaerobic carnitine reduction. May bring reductant to CaiA. (256 aa)
fixBProtein FixB; Required for anaerobic carnitine reduction. May bring reductant to CaiA. (313 aa)
aceEPyruvate dehydrogenase, decarboxylase component E1, thiamin-binding; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (887 aa)
aceFPyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (630 aa)
lpdLipoamide dehydrogenase, E3 component is part of three enzyme complexes; Function experimentally demonstrated in the studied species; enzyme. (474 aa)
acnBBifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aconitase/IPM isomerase family. (865 aa)
cyoACytochrome o ubiquinol oxidase subunit II; Function experimentally demonstrated in the studied species; carrier. (315 aa)
cyoBCytochrome o ubiquinol oxidase subunit I; Function experimentally demonstrated in the studied species; carrier; Belongs to the heme-copper respiratory oxidase family. (663 aa)
cyoCCytochrome o ubiquinol oxidase subunit III; Function experimentally demonstrated in the studied species; carrier. (204 aa)
cyoDCytochrome o ubiquinol oxidase subunit IV; Function experimentally demonstrated in the studied species; carrier. (109 aa)
frmAAlcohol dehydrogenase class III/glutathione-dependent formaldehyde dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. (369 aa)
prpD2-methylcitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme. (483 aa)
fdoHFormate dehydrogenase-O, Fe-S subunit; The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. (300 aa)
fdoIFormate dehydrogenase-O, cytochrome b556 subunit; Function experimentally demonstrated in the studied species; carrier. (211 aa)
hemGProtoporphyrin oxidase, flavoprotein; Function experimentally demonstrated in the studied species; carrier. (181 aa)
ubiEUbiquinone/menaquinone biosynthesis C-methyltransferase UbiE; Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3- methyl-6-methoxy-1,4-benzoquinol (DMQH2). (251 aa)
enoEnolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. (432 aa)
yqcAPutative flavoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (149 aa)
ygfSPutative oxidoreductase, 4Fe-4S ferredoxin-type subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (162 aa)
fldBFlavodoxin 2; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. (173 aa)
rpiARibose 5-phosphate isomerase, constitutive; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. (219 aa)
fbaAFructose-bisphosphate aldolase, class II; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis; Belongs to the class II fructose-bisphosphate aldolase family. (359 aa)
pgkPhosphoglycerate kinase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the phosphoglycerate kinase family. (387 aa)
tktATransketolase 1, thiamin-binding; 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. (663 aa)
glcBMalate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. (723 aa)
hybCHydrogenase 2, large subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (567 aa)
yahGConserved hypothetical protein; Homologs of previously reported genes of unknown function. (472 aa)
prpC2-methylcitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (389 aa)
lsrFPutative aldolase; Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the transfer of an acetyl moiety from 3-hydroxy-5- phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and acetyl-CoA; Belongs to the DeoC/FbaB aldolase family. (291 aa)
dsbBOxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. (176 aa)
icd-2Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. (416 aa)
ycfZConserved hypothetical protein; Homologs of previously reported genes of unknown function; putative membrane component. (262 aa)
yceJPutative cytochrome b561; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (188 aa)
torATrimethylamine N-oxide (TMAO) reductase I, catalytic subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (848 aa)
hybBFunction of strongly homologous gene; carrier. (392 aa)
hybAHydrogenase 2 4Fe-4S ferredoxin-type component; Function experimentally demonstrated in the studied species; putative carrier. (328 aa)
hybOHydrogenase 2, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 aa)
mdhMalate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
rpeD-ribulose-5-phosphate 3-epimerase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the ribulose-phosphate 3-epimerase family. (225 aa)
glgAGlycogen synthase; Synthesizes alpha-1,4-glucan chains using ADP-glucose. (477 aa)
glgCGlucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc. (431 aa)
glgXGlycogen debranching enzyme; Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin. (657 aa)
glgB1,4-alpha-glucan branching enzyme; Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position; Belongs to the glycosyl hydrolase 13 family. GlgB subfamily. (728 aa)
yhjACytochrome C peroxidase (cpp-like); Function experimentally demonstrated in the studied species; enzyme. (465 aa)
bisCBiotin sulfoxide reductase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (759 aa)
yiaIPutative hydrogenase, 4Fe-4S ferredoxin-type component; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (157 aa)
gpmIPhosphoglycero mutase III, cofactor-independent; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. (514 aa)
aceBMalate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. (533 aa)
aceAIsocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. (434 aa)
aceKIsocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. (574 aa)
pgiGlucosephosphate isomerase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the GPI family. (549 aa)
nrfANitrite reductase, formate-dependent, cytochrome; Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process; Belongs to the cytochrome c-552 family. (478 aa)
nrfBNitrite reductase, formate-dependent, penta-heme cytochrome c; Function experimentally demonstrated in the studied species; carrier. (188 aa)
nrfCFormate-dependent nitrite reductase, 4Fe4S subunit; Function experimentally demonstrated in the studied species; carrier. (223 aa)
alsEAllulose-6-phosphate 3-epimerase; Function experimentally demonstrated in the studied species; enzyme. (231 aa)
fumBAnaerobic class I fumarate hydratase (fumarase B); Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (548 aa)
dipZFused thiol:disulfide interchange protein: activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. (565 aa)
aspAAspartate ammonia-lyase; Function experimentally demonstrated in the studied species; enzyme. (478 aa)
yjeKPutative lysine aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (342 aa)
frdCFumarate reductase (anaerobic), membrane anchor subunit; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (131 aa)
frdBFumarate reductase (anaerobic), Fe-S subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (244 aa)
frdAFumarate reductase (anaerobic) catalytic and NAD/flavoprotein subunit; Function experimentally demonstrated in the studied species; enzyme. (602 aa)
CAR20769.1Putative CoA transferase; CoA transferase having broad substrate specificity for short- chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Belongs to the 3-oxoacid CoA-transferase family. (513 aa)
cybCSoluble cytochrome b562; Function experimentally demonstrated in the studied species; carrier. (128 aa)
nrdGAnaerobic ribonucleotide reductase activating protein; Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine. (154 aa)
hgdCATPase, activator of (R)-hydroxyglutaryl-CoA dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (255 aa)
ytjCPhosphoglyceromutase 2, co-factor independent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the phosphoglycerate mutase family. GpmB subfamily. (215 aa)
fumCFumarate hydratase (fumarase C),aerobic Class II; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (467 aa)
fumAFumarate hydratase (fumarase A), aerobic Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (548 aa)
rsxAPutative inner membrane subunit of an electron transport system; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. (193 aa)
rsxBPutative iron-sulfur protein; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR; Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily. (192 aa)
rsxCPutative 4Fe-4S ferredoxin-type protein fused with unknown protein; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR; Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily. (740 aa)
rsxDPutative inner membrane oxidoreductase; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR; Belongs to the NqrB/RnfD family. (352 aa)
rsxGPutative oxidoreductase; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR; Belongs to the RnfG family. (206 aa)
rsxEPutative inner membrane NADH-quinone reductase; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. (231 aa)
ydhUPutative cytochrome b subunit of a reductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (261 aa)
ydhVPutative ferredoxin:oxidoreductase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (700 aa)
ydhYPutative 4Fe-4S ferridoxin-type subunit of oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (208 aa)
pntBPyridine nucleotide transhydrogenase, beta subunit; The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane; Belongs to the PNT beta subunit family. (462 aa)
pykFPyruvate kinase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (470 aa)
ydiFFragment of putative acyl-CoA dehydrogenase (part 1); CoA transferase having broad substrate specificity for short- chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Belongs to the 3-oxoacid CoA-transferase family. (531 aa)
ydiQPutative electron transfer flavoprotein subunit (etfB-like); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (254 aa)
ydiRPutative electron transfer flavoprotein subunit, FAD-binding; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (312 aa)
gapAGlyceraldehyde-3-phosphate dehydrogenase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. (331 aa)
zwfGlucose-6-phosphate dehydrogenase; Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone. (491 aa)
pykAPyruvate kinase II; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (480 aa)
torZTrimethylamine N-oxide reductase system III, catalytic subunit; Function experimentally demonstrated in the studied species; enzyme. (809 aa)
torYTMAO reductase III (TorYZ), cytochrome c-type subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the TorC/TorY family. (366 aa)
yedZHeme-molybdoenzyme heme-containing subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipo [...] (211 aa)
gndGluconate-6-phosphate dehydrogenase, decarboxylating; Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. (468 aa)
fbaBFructose-bisphosphate aldolase class I; Function experimentally demonstrated in the studied species; enzyme. (350 aa)
dldD-lactate dehydrogenase, FAD-binding, NADH independent; Catalyzes the oxidation of D-lactate to pyruvate. Belongs to the quinone-dependent D-lactate dehydrogenase family. (585 aa)
grxAGlutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); Function experimentally demonstrated in the studied species; carrier. (85 aa)
ybhJPutative enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (674 aa)
pgl6-phosphogluconolactonase; Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate. (331 aa)
gpmAPhosphoglyceromutase 1; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily. (250 aa)
cydBCytochrome d terminal oxidase, subunit II; Function experimentally demonstrated in the studied species; carrier. (379 aa)
cydACytochrome d terminal oxidase, subunit I; Function experimentally demonstrated in the studied species; carrier. (522 aa)
glmS-2Methylaspartate mutase S chain (Glutamate mutase sigma subunit); Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). (170 aa)
glmEMethylaspartate mutase E chain (Glutamate mutase epsilon subunit); Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). (481 aa)
CAR16834.1Fumarate hydratase class I, beta subunit, aerobic (Fumarase); Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (550 aa)
sucDsuccinyl-CoA synthetase, NAD(P)-binding, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (289 aa)
sucCsuccinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (388 aa)
sucBDihydrolipoyltranssuccinase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). (405 aa)
yahFPutative enzyme with acyl-CoA domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (515 aa)
ykgEPutative hydroxyacid oxidoreductase (Fe-S centre); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (239 aa)
fdrAPutative acyl-CoA synthetase with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (555 aa)
ylbEConserved hypothetical protein; Homologs of previously reported genes of unknown function. (419 aa)
ybdHPutative oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (362 aa)
fldAFlavodoxin 1; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. (176 aa)
gltACitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (427 aa)
sdhCSuccinate dehydrogenase, membrane subunit, binds cytochrome b556; Function experimentally demonstrated in the studied species; membrane component. (129 aa)
sdhDSuccinate dehydrogenase, membrane subunit, binds cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (115 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa)
sdhBSuccinate dehydrogenase, FeS subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (238 aa)
sucA2-oxoglutarate decarboxylase, thiamin-requiring; Function experimentally demonstrated in the studied species; enzyme. (933 aa)
ynfHOxidoreductase, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (284 aa)
ynfGOxidoreductase, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (205 aa)
ynfFOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (807 aa)
ynfEOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (808 aa)
acnAAconitate hydratase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (891 aa)
ydbKPutative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (1174 aa)
ldhAFermentative D-lactate dehydrogenase, NAD-dependent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (329 aa)
azoRNADH-azoreductase, FMN-dependent; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (201 aa)
fdnGFormate dehydrogenase-N, alpha subunit, nitrate-inducible; Function experimentally demonstrated in the studied genus; enzyme. (1015 aa)
fdnHFormate dehydrogenase-N, Fe-S (beta) subunit, nitrate-inducible; The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. (294 aa)
fdnIFormate dehydrogenase-N, cytochrome B556 (gamma) subunit, nitrate-inducible; Function experimentally demonstrated in the studied species; carrier. (217 aa)
torCTrimethylamine N-oxide (TMAO) reductase I, cytochrome c-type subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the TorC/TorY family. (390 aa)
torTPeriplasmic sensory protein associated with the TorRS two-component regulatory system; Function experimentally demonstrated in the studied species; regulator. (342 aa)
appBCytochrome bd-II oxidase, subunit II; Function experimentally demonstrated in the studied species; carrier. (378 aa)
appCCytochrome bd-II oxidase, subunit I; Function experimentally demonstrated in the studied species; carrier. (514 aa)
hyaCHydrogenase 1, b-type cytochrome subunit; Function experimentally demonstrated in the studied species; carrier. (235 aa)
hyaBHydrogenase 1, large subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (597 aa)
hyaAHydrogenase 1, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 aa)
dmsCDimethyl sulfoxide reductase, anaerobic, subunit C; Function experimentally demonstrated in the studied species; enzyme. (287 aa)
dmsBDimethyl sulfoxide reductase, anaerobic, subunit B; Function experimentally demonstrated in the studied species; enzyme. (205 aa)
dmsADimethyl sulfoxide reductase, anaerobic, subunit A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (814 aa)
yeiBConserved hypothetical protein; Homologs of previously reported genes of unknown function; putative membrane component. (385 aa)
napCNitrate reductase, cytochrome c-type,periplasmic; Function experimentally demonstrated in the studied species; carrier. (200 aa)
napBNitrate reductase, small, cytochrome C550 subunit, periplasmic; Electron transfer subunit of the periplasmic nitrate reductase complex NapAB; Belongs to the NapB family. (149 aa)
napGQuinol dehydrogenase periplasmic component; Function experimentally demonstrated in the studied species; carrier. (231 aa)
napANitrate reductase, periplasmic, large subunit; Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite. (828 aa)
mqoMalate dehydrogenase, FAD/NAD(P)-binding domain; Function experimentally demonstrated in the studied species; enzyme. (548 aa)
yfaEPutative 2Fe-2S cluster-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (84 aa)
glpCSn-glycerol-3-phosphate dehydrogenase (anaerobic), small subunit; Function experimentally demonstrated in the studied species; enzyme. (396 aa)
nuoNNADH:ubiquinone oxidoreductase, membrane subunit N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (485 aa)
nuoMNADH:ubiquinone oxidoreductase, membrane subunit M; Function experimentally demonstrated in the studied species; membrane component. (509 aa)
nuoLNADH:ubiquinone oxidoreductase, membrane subunit L; Function experimentally demonstrated in the studied species; membrane component. (613 aa)
nuoKNADH:ubiquinone oxidoreductase, membrane subunit K; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (100 aa)
nuoJNADH:ubiquinone oxidoreductase, membrane subunit J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (184 aa)
nuoINADH:ubiquinone oxidoreductase, chain I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (180 aa)
nuoHNADH:ubiquinone oxidoreductase, membrane subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (325 aa)
nuoGNADH:ubiquinone oxidoreductase, chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. (910 aa)
nuoFNADH:ubiquinone oxidoreductase, chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (445 aa)
nuoENADH:ubiquinone oxidoreductase, chain E; Function experimentally demonstrated in the studied species; carrier. (166 aa)
nuoCNADH:ubiquinone oxidoreductase, chain C,D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (600 aa)
nuoBNADH:ubiquinone oxidoreductase, chain B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (220 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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