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aceE aceE aceF aceF accA accA prpR prpR prpB prpB prpC prpC prpD prpD prpE prpE ybiW ybiW ybiY ybiY fsaA fsaA pflA pflA pflB pflB adhE adhE ackA ackA pta pta accD accD eutI eutI yfiD yfiD tdcE tdcE tdcD tdcD yhdH yhdH accB accB accC accC acs acs
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
aceEPyruvate dehydrogenase, decarboxylase component E1, thiamin-binding; Function experimentally demonstrated in the studied species; enzyme. (887 aa)
aceFPyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; Function experimentally demonstrated in the studied species; enzyme. (630 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)
prpRDNA-binding transcriptional activator; Function experimentally demonstrated in the studied species; regulator. (528 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)
prpC2-methylcitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (389 aa)
prpD2-methylcitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme. (483 aa)
prpEpropionyl-CoA synthetase; Function of homologous gene experimentally demonstrated in an other organism; putative enzyme. (628 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)
fsaAFructose-6-phosphate aldolase 1; Function experimentally demonstrated in the studied species; enzyme. (220 aa)
pflAPyruvate formate lyase activating enzyme 1; Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (246 aa)
pflBPyruvate formate lyase I; Function experimentally demonstrated in the studied species; enzyme. (760 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)
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; Function experimentally demonstrated in the studied species; enzyme. (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)
eutIPutative phosphotransacetylase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (338 aa)
yfiDPyruvate formate lyase subunit; Acts as a radical domain for damaged PFL and possibly other radical proteins. (127 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)
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; Function experimentally demonstrated in the studied species; enzyme. (449 aa)
acsacetyl-CoA synthetase; Function experimentally demonstrated in the studied species; enzyme. (652 aa)
Your Current Organism:
Escherichia coli IAI1
NCBI taxonomy Id: 585034
Other names: E. coli IAI1, Escherichia coli str. IAI1, Escherichia coli strain IAI1
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