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pflB pflB lipA lipA miaB miaB bioB bioB moaA moaA moaB moaB moaC moaC moaD moaD moaE moaE rimO rimO fnr fnr fumA fumA edd edd hypB hypB hypD hypD scpA scpA tdcE tdcE aslB aslB hemN hemN tpiA tpiA thiH thiH thiG thiG thiC thiC zraR zraR metH metH soxR soxR fumB fumB epmB epmB
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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
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a 3D structure is known or predicted
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pflBFormate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. (760 aa)
lipALipoate synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. Free octanoate is not a substrate for LipA; Belongs to the radical SAM superfamily. Lipoyl synthase family. (321 aa)
miaBtRNA-i(6)A37 methylthiotransferase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (474 aa)
bioBBiotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. (346 aa)
moaAMolybdopterin biosynthesis protein A; Catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z). (329 aa)
moaBInactive molybdopterin adenylyltransferase; May be involved in the biosynthesis of molybdopterin. Can bind GTP and has low GTPase activity. Can bind MPT, but has no MPT adenylyl transferase activity; Belongs to the MoaB/Mog family. (170 aa)
moaCMolybdopterin biosynthesis, protein C; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). (161 aa)
moaDMolybdopterin synthase, small subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Belongs to the MoaD family. (81 aa)
moaEMolybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. (150 aa)
rimORibosomal protein S12 methylthiotransferase; Catalyzes the methylthiolation of the residue Asp-89 of ribosomal protein S12. (441 aa)
fnrOxygen-sensing anaerobic growth regulon transcriptional regulator FNR; Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O(2), is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration. (250 aa)
fumAFumarate hydratase (fumarase A), aerobic Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate. (548 aa)
edd6-phosphogluconate dehydratase; Catalyzes the dehydration of 6-phospho-D-gluconate to 2- dehydro-3-deoxy-6-phospho-D-gluconate. (603 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)
hypDHydrogenase maturation protein; Involved in the maturation of [NiFe] hydrogenases. Involved in the biosynthesis of the Fe(CN)(2)CO cofactor. HypD may act as a scaffold on which the Fe(CN)(2)CO cofactor is formed. In complex with HypC, accepts the cyanide ligand generated by HypF and HypE, and also coordinates the carbon monoxide ligand. Required for the formation of all three hydrogenase isoenzymes (Probable). (373 aa)
scpAmethylmalonyl-CoA mutase; Catalyzes the interconversion of succinyl-CoA and methylmalonyl-CoA. Could be part of a pathway that converts succinate to propionate. (714 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)
aslBPutative AslA-specific sulfatase-maturating enzyme; Putative arylsulfatase regulator; Protein involved in sulfur metabolic process and protein folding; Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family. (411 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)
thiHTyrosine lyase, involved in thiamine-thiazole moiety synthesis; Catalyzes the radical-mediated cleavage of tyrosine to 2- iminoacetate and 4-cresol. (377 aa)
thiGThiamine biosynthesis ThiGH complex subunit; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S; Belongs to the ThiG family. (256 aa)
thiCPhosphomethylpyrimidine synthase; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. (631 aa)
zraRTranscriptional regulatory protein ZraR; Member of the two-component regulatory system ZraS/ZraR. When activated by ZraS it acts in conjunction with sigma-54 to regulate the expression of zraP. Positively autoregulates the expression of the zraSR operon. (441 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)
soxRRedox-sensitive transcriptional activator of soxS; Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron- sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress. Upon reduction of 2Fe-2S cluster, SoxR reversibly loses its transcriptional activity, but retains its DNA binding affinity. (154 aa)
fumBAnaerobic class I fumarate hydratase (fumarase B); Catalyzes the reversible hydration of fumarate to (S)-malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D-tartrate dehydratase activity, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Is required for anaerobic growth on D-tartrate. Belongs to the class-I fumarase family. (548 aa)
epmBEF-P-Lys34 lysylation protein; With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3- aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine). Cannot use (S)-ornithine or (R)-alpha-lysine as a substrate; Belongs to the radical SAM superfamily. KamA family. (342 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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