STRINGSTRING
pflC pflC ybiY ybiY pflA pflA pflB pflB adhE adhE eutG eutG hypB hypB queE queE tdcE tdcE yiaY yiaY hemN hemN tpiA tpiA metH metH groL groL
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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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query proteins and first shell of interactors
white nodes:
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
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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pflCPutative [formate-C-acetyltransferase 2]-activating enzyme; Activation of pyruvate formate-lyase 2 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. (292 aa)
ybiYPutative pyruvate formate lyase activating enzyme; Activation of pyruvate formate-lyase 2 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. (299 aa)
pflAPyruvate formate-lyase 1-activating enzyme; Activation of pyruvate formate-lyase 1 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)
pflBFormate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. (760 aa)
adhEAcetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. (891 aa)
eutGEthanol dehydrogenase involved in ethanolamine utilization; May act on the acetaldehyde produced from the degradation of ethanolamine; Belongs to the iron-containing alcohol dehydrogenase family. (395 aa)
hypBGTP hydrolase involved in nickel liganding into hydrogenases; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion. In the presence of GDP, nickel, but not zinc, is transferred from the HypB GTPase domain (G-domain) to HypA. Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily. (290 aa)
queE7-carboxy-7-deazaguanine synthase; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (223 aa)
tdcEPyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate. Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily. (764 aa)
yiaYL-threonine dehydrogenase; Putative oxidoreductase. (383 aa)
hemNCoproporphyrinogen III oxidase, SAM and NAD(P)H dependent, oxygen-independent; Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX. It can use NAD or NADP, but NAD is preferred. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (457 aa)
tpiATriosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (255 aa)
metHhomocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. (1227 aa)
groLCpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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