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mreB mreB gntR gntR tpiA tpiA rpiB rpiB yfeX yfeX hemF hemF eutR eutR eutG eutG adhE adhE moeB moeB eutD eutD eutQ eutQ eutT eutT eutJ eutJ eutP eutP maeB maeB
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query proteins and first shell of interactors
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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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mreBCell wall structural complex MreBCD, actin-like component MreB; Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization maintains elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polyme [...] (347 aa)
gntRD-gluconate inducible gluconate regulon transcriptional repressor; Negative regulator for the gluconate utilization system GNT- I, the gntUKR operon. (331 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)
rpiBRibose 5-phosphate isomerase B/allose 6-phosphate isomerase; Catalyzes the interconversion of ribulose-5-P and ribose-5-P. It probably also has activity on D-allose 6-phosphate. (149 aa)
yfeXPorphyrinogen oxidase, cytoplasmic; Has both general peroxidase activity and dye-decolorizing activity. Can catalyze the oxidation of both protoporphyrinogen IX and coproporphyrinogen III to their corresponding porphyrins. Also efficiently decolorizes the dyes alizarin red and Cibacron blue F3GA. (299 aa)
hemFCoproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. (299 aa)
eutREut operon transcriptional activator, AraC family; Activates the transcription of the eut operon. Also positively regulates its own transcription. Probably binds ethanolamine and vitamin B12 as effectors (By similarity). (350 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)
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)
moeBMolybdopterin synthase sulfurylase; Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD. (249 aa)
eutDPhosphate acetyltransferase; Ethanolamine utilization; homolog of Salmonella acetyl/butyryl P transferase; Protein involved in amine catabolic process. (338 aa)
eutQRmlC-like cupin domain protein; Protein involved in amine catabolic process. (233 aa)
eutTCobalamin adenosyltransferase involved in ethanolamine utilization; Converts CNB12 to ADOB12. (267 aa)
eutJEthanolamine utilization; homolog of Salmonella gene; Protein involved in amine catabolic process and protein folding. (278 aa)
eutPPutative P-loop NTPase ethanolamine utilization protein; Protein involved in amine catabolic process. (159 aa)
maeBMalic enzyme: putative oxidoreductase/phosphotransacetylase; Putative multimodular enzyme; In the N-terminal section; belongs to the malic enzymes family. (759 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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