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lpd lpd acnB acnB gcl gcl hyi hyi glxR glxR glxK glxK gltA gltA ybhJ ybhJ ycdW ycdW purU purU acnA acnA aldA aldA CAQ98346.1 CAQ98346.1 katE katE yeaU yeaU eda eda oxc oxc glyA glyA fucO fucO yqeF yqeF gcvP gcvP gcvH gcvH gcvT gcvT yliK yliK glcB glcB glcF glcF glcE glcE glcD glcD ttdA ttdA ttdB ttdB garK garK garR garR mdh mdh gph gph tiaE tiaE glnA glnA fdoI fdoI fdoH fdoH fdoG fdoG aceB aceB aceA aceA 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:
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. (865 aa)
gclGlyoxylate carboligase; Function experimentally demonstrated in the studied species; enzyme. (593 aa)
hyiHydroxypyruvate isomerase; Function experimentally demonstrated in the studied species; enzyme. (258 aa)
glxRTartronate semialdehyde reductase, NADH-dependent; Function experimentally demonstrated in the studied species; enzyme. (292 aa)
glxKGlycerate kinase II; Function experimentally demonstrated in the studied species; enzyme. (381 aa)
gltACitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (427 aa)
ybhJPutative enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (753 aa)
ycdW2-ketoacid reductase; Function experimentally demonstrated in the studied species; enzyme. (312 aa)
purUtRNA-Tyr; Gene remnant. (280 aa)
acnAAconitate hydratase 1; Function experimentally demonstrated in the studied species; enzyme. (891 aa)
aldAAldehyde dehydrogenase A, NAD-linked; Function experimentally demonstrated in the studied species; enzyme. (479 aa)
CAQ98346.1Putative acetyl-CoA acetyltransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (401 aa)
katEHydroperoxidase HPII(III) (catalase); Serves to protect cells from the toxic effects of hydrogen peroxide. (753 aa)
yeaUPutative tartrate dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (361 aa)
eda2-dehydro-3-deoxyphosphogluconate aldolase / (4S)-4-hydroxy-2-oxoglutarate aldolase; Function experimentally demonstrated in the studied species; enzyme. (213 aa)
oxcPutative oxalyl-CoA decarboxylase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (564 aa)
glyASerine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (417 aa)
fucOL-1,2-propanediol oxidoreductase; Function experimentally demonstrated in the studied species; enzyme. (383 aa)
yqeFAcetyl-CoA acetyltransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (393 aa)
gcvPGlycine decarboxylase, PLP-dependent, subunit (protein P) of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. (957 aa)
gcvHGlycine cleavage complex lipoylprotein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. (129 aa)
gcvTAminomethyltransferase, tetrahydrofolate-dependent, subunit (T protein) of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. (364 aa)
yliKmethylmalonyl-CoA mutase; Function experimentally demonstrated in the studied species; enzyme. (714 aa)
glcBMalate synthase G; Function experimentally demonstrated in the studied species; enzyme. (723 aa)
glcFGlycolate oxidase iron-sulfur subunit; Function experimentally demonstrated in the studied species; carrier. (407 aa)
glcEGlycolate oxidase FAD binding subunit; Function experimentally demonstrated in the studied species; enzyme. (350 aa)
glcDGlycolate oxidase subunit, FAD-linked; Function experimentally demonstrated in the studied species; enzyme. (499 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)
garKGlycerate kinase I; Function experimentally demonstrated in the studied species; enzyme. (408 aa)
garRTartronate semialdehyde reductase; Function experimentally demonstrated in the studied species; enzyme. (296 aa)
mdhMalate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
gphPhosphoglycolate phosphatase; Function experimentally demonstrated in the studied species; enzyme. (252 aa)
tiaE2-oxo-carboxylic acid reductase (glyoxalate reductase) (2-ketoaldonate reductase); Function experimentally demonstrated in the studied species; enzyme. (324 aa)
glnAGlutamine synthetase; Function experimentally demonstrated in the studied species; enzyme. (469 aa)
fdoIFormate dehydrogenase-O, cytochrome b556 subunit; Function experimentally demonstrated in the studied species; carrier. (211 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)
fdoGFormate dehydrogenase-O, large subunit; Function experimentally demonstrated in the studied genus; enzyme. (1016 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)
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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