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cutD cutD pykF pykF pps pps pykA pykA poxB poxB panD panD speD speD aceF aceF aceE aceE adhE adhE pflB pflB pflA pflA sseA sseA pflC pflC pflD pflD tdcE tdcE murA murA avtA avtA adhE-3 adhE-3 yjjW yjjW psd psd ubiC ubiC
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:
cutDPutative pyruvate formate-lyase activating enzyme; Catalyzes activation of the choline trimethylamine-lyase CutC under anaerobic conditions by generation of an organic free radical on a glycine residue, via an homolytic cleavage of S-adenosyl-L-methionine (SAM). (315 aa)
pykFPyruvate kinase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (470 aa)
ppsPhosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family. (792 aa)
pykAPyruvate kinase II; Function experimentally demonstrated in the studied species; enzyme; Belongs to the pyruvate kinase family. (480 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)
panDAspartate 1-decarboxylase; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. (126 aa)
speDS-adenosylmethionine decarboxylase; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily. (264 aa)
aceFPyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (630 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)
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)
pflBPyruvate formate lyase I; Function experimentally demonstrated in the studied species; enzyme. (760 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)
sseA3-mercaptopyruvate sulfurtransferase; Function experimentally demonstrated in the studied species; enzyme. (281 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)
tdcEPyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Function experimentally demonstrated in the studied species; enzyme. (764 aa)
murAUDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily. (419 aa)
avtAValine-pyruvate aminotransferase; Function experimentally demonstrated in the studied species; enzyme. (417 aa)
adhE-3Fragment of fused acetaldehyde-CoA dehydrogenase; Glycine radical enzyme that catalyzes the cleavage of a C-N bond in choline, producing trimethylamine (TMA) and acetaldehyde. Belongs to the glycyl radical enzyme (GRE) family. CutC subfamily. (1140 aa)
yjjWPutative pyruvate formate lyase activating enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (287 aa)
psdPhosphatidylserine decarboxylase; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). (322 aa)
ubiCChorismate pyruvate lyase; Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. (165 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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