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leuD leuD leuC leuC leuB leuB leuA leuA ilvI ilvI ilvH ilvH aceE aceE aceF aceF lpd lpd acnB acnB accA accA prpE prpE prpD prpD prpC prpC prpB prpB fadE fadE gltA gltA sdhC sdhC sdhD sdhD sdhA sdhA sdhB sdhB sucA sucA sucB sucB sucC sucC sucD sucD CAR16834.1 CAR16834.1 ybhJ ybhJ ybiW ybiW ybiY ybiY poxB poxB dld dld pykA pykA fadD fadD yeaU yeaU pps pps pykF pykF ydhZ ydhZ fumA fumA fumC fumC adhE adhE acnA acnA ldhA ldhA sfcA sfcA icd-2 icd-2 pflB pflB mqo mqo ackA ackA pta pta accD accD yfcX yfcX yfcY yfcY fadL fadL eutI eutI maeB maeB ilvC ilvC ilvA ilvA ilvD ilvD ilvE ilvE ilvM ilvM ilvG ilvG ppc ppc pflC pflC pflD pflD fadB fadB fadA fadA yqeF yqeF yliK yliK argK argK ygfG ygfG ygfH ygfH yggD yggD ygiP ygiP ttdA ttdA ttdB ttdB ygjE ygjE fadH fadH tdcE tdcE tdcD tdcD mdh mdh yhdH yhdH accB accB accC accC pck pck ilvN ilvN ilvB ilvB acs acs fumB fumB frdD frdD frdC frdC frdB frdB frdA frdA CAR20769.1 CAR20769.1 CAR20770.1 CAR20770.1
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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leuD3-isopropylmalate isomerase subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. (201 aa)
leuC3-isopropylmalate isomerase subunit, dehydratase component; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (466 aa)
leuB3-isopropylmalate dehydrogenase; 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. (363 aa)
leuA2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. (523 aa)
ilvIAcetolactate synthase III, large subunit; Function experimentally demonstrated in the studied species; enzyme. (574 aa)
ilvHAcetolactate synthase III, thiamin-dependent, small subunit; Function experimentally demonstrated in the studied species; enzyme. (163 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)
accAacetyl-CoA carboxylase, carboxytransferase, alpha subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. (319 aa)
prpEpropionyl-CoA synthetase; Function of homologous gene experimentally demonstrated in an other organism; putative enzyme. (628 aa)
prpD2-methylcitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme. (483 aa)
prpC2-methylcitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (389 aa)
prpB2-methylisocitrate lyase; Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate. Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family. (296 aa)
fadEAcyl coenzyme A dehydrogenase; Function experimentally demonstrated in the studied species; enzyme. (814 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)
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)
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)
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)
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)
ybhJPutative enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (674 aa)
ybiWPutative glycyl radical cofactor protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (810 aa)
ybiYPutative AdoMet-dependent glycyl radical activating enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (308 aa)
poxBPyruvate dehydrogenase (pyruvate oxidase), thiamin-dependent, FAD-binding; Function experimentally demonstrated in the studied species; enzyme; Belongs to the TPP enzyme family. (572 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)
pykAPyruvate kinase II; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (480 aa)
fadDacyl-CoA synthetase (long-chain-fatty-acid--CoA ligase); Function experimentally demonstrated in the studied species; enzyme. (561 aa)
yeaUPutative tartrate dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (361 aa)
ppsPhosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family. (792 aa)
pykFPyruvate kinase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (470 aa)
ydhZConserved hypothetical protein; Homologs of previously reported genes of unknown function. (69 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)
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)
adhEFused acetaldehyde-CoA dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. (891 aa)
acnAAconitate hydratase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (891 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)
sfcAMalate dehydrogenase, (decarboxylating, NAD-requiring) (malic enzyme); Function experimentally demonstrated in the studied species; enzyme; Belongs to the malic enzymes family. (565 aa)
icd-2Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. (416 aa)
pflBPyruvate formate lyase I; Function experimentally demonstrated in the studied species; enzyme. (760 aa)
mqoMalate dehydrogenase, FAD/NAD(P)-binding domain; Function experimentally demonstrated in the studied species; enzyme. (548 aa)
ackAAcetate kinase A and propionate kinase 2; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family. (400 aa)
ptaPhosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family. (714 aa)
accDacetyl-CoA carboxylase, beta (carboxyltranferase) subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA; Belongs to the AccD/PCCB family. (304 aa)
yfcXFused enoyl-CoA hydratase and epimerase and isomerase; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (714 aa)
yfcYbeta-ketoacyl-CoA thiolase, anaerobic, subunit; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. (436 aa)
fadLLong-chain fatty acid outer membrane transporter; Function experimentally demonstrated in the studied species; transporter. (448 aa)
eutIPutative phosphotransacetylase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (338 aa)
maeBPutative fused malic enzyme oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (759 aa)
ilvCKetol-acid reductoisomerase, NAD(P)-binding; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. (491 aa)
ilvAThreonine deaminase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. (514 aa)
ilvDDihydroxyacid dehydratase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the IlvD/Edd family. (616 aa)
ilvEBranched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (309 aa)
ilvMAcetolactate synthase II, small subunit; Function experimentally demonstrated in the studied species; enzyme. (87 aa)
ilvGAcetolactate synthase; Function of strongly homologous gene; enzyme. (548 aa)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. (883 aa)
pflCPyruvate formate lyase II activase; Function experimentally demonstrated in the studied species; enzyme. (292 aa)
pflDPutative formate acetyltransferase 2 (pyruvate formate lyase II); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (765 aa)
fadBEnoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (729 aa)
fadA3-ketoacyl-CoA thiolase (thiolase I); Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. (387 aa)
yqeFAcetyl-CoA acetyltransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the thiolase-like superfamily. Thiolase family. (393 aa)
yliKmethylmalonyl-CoA mutase; Function experimentally demonstrated in the studied species; enzyme. (714 aa)
argKMembrane ATPase/protein kinase; Function experimentally demonstrated in the studied species; transporter. (331 aa)
ygfGmethylmalonyl-CoA decarboxylase, biotin-independent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the enoyl-CoA hydratase/isomerase family. (261 aa)
ygfHpropionyl-CoA:succinate-CoA transferase; Function experimentally demonstrated in the studied species; enzyme. (492 aa)
yggDPutative DNA-binding transcriptional regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (169 aa)
ygiPPutative DNA-binding transcriptional regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator; Belongs to the LysR transcriptional regulatory family. (310 aa)
ttdAL-tartrate dehydratase, alpha subunit; Function experimentally demonstrated in the studied species; enzyme. (303 aa)
ttdBL-tartrate dehydratase, beta subunit; Function experimentally demonstrated in the studied species; enzyme. (201 aa)
ygjEPutative tartrate:succinate antiporter; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (487 aa)
fadH2,4-dienoyl-CoA reductase, NADH and FMN-linked; Function experimentally demonstrated in the studied species; enzyme. (672 aa)
tdcEPyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Function experimentally demonstrated in the studied species; enzyme. (764 aa)
tdcDPropionate kinase/acetate kinase C, anaerobic; Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. (406 aa)
mdhMalate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
yhdHPutative oxidoreductase, Zn-dependent and NAD(P)-binding; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (324 aa)
accBAcetyl CoA carboxylase, BCCP subunit; 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. (156 aa)
accCacetyl-CoA carboxylase, biotin carboxylase subunit; 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. (449 aa)
pckPhosphoenolpyruvate carboxykinase; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. Belongs to the phosphoenolpyruvate carboxykinase (ATP) family. (540 aa)
ilvNAcetolactate synthase I, small subunit; Function experimentally demonstrated in the studied species; enzyme. (96 aa)
ilvBAcetolactate synthase I, large subunit; Function experimentally demonstrated in the studied species; enzyme. (562 aa)
acsacetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. (652 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)
frdDFumarate 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. (119 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)
CAR20770.1Putative acyl-CoA hydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the enoyl-CoA hydratase/isomerase family. (258 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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