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aceA aceA acnB acnB yahF yahF yahG yahG prpC prpC prpD prpD fdrA fdrA ylbE ylbE gltA gltA sdhC sdhC sdhD sdhD aceB aceB sdhA sdhA sdhB sdhB sucA sucA sucB sucB sucC sucC sucD sucD ybhJ ybhJ icd icd acnA acnA fumC fumC fumA fumA mqo mqo glcB glcB mdh mdh ppc ppc aspA aspA aceK aceK frdB frdB
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.
Node Color
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:
aceAIsocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. (434 aa)
acnBBifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme. (865 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)
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)
prpD2-methylcitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme. (483 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)
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)
aceBMalate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. (533 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. (238 aa)
sucA2-oxoglutarate decarboxylase, thiamin-requiring; Function experimentally demonstrated in the studied species; enzyme. (933 aa)
sucBDihydrolipoyltranssuccinase; Function experimentally demonstrated in the studied species; enzyme. (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)
ybhJPutative enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (753 aa)
icdIsocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. (416 aa)
acnAAconitate hydratase 1; Function experimentally demonstrated in the studied species; enzyme. (891 aa)
fumCFumarate hydratase (fumarase C),aerobic Class II; Function experimentally demonstrated in the studied species; enzyme. (467 aa)
fumAFumarate hydratase (fumarase A), aerobic Class I; Function experimentally demonstrated in the studied species; enzyme. (548 aa)
mqoMalate dehydrogenase, FAD/NAD(P)-binding domain; Function experimentally demonstrated in the studied species; enzyme. (548 aa)
glcBMalate synthase G; Function experimentally demonstrated in the studied species; enzyme. (723 aa)
mdhMalate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family. (883 aa)
aspAAspartate ammonia-lyase; Function experimentally demonstrated in the studied species; enzyme. (478 aa)
aceKIsocitrate dehydrogenase kinase/phosphatase; Function experimentally demonstrated in the studied species; enzyme. (578 aa)
frdBFumarate reductase (anaerobic), Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (244 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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