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ybiY ybiY lipA lipA miaB miaB bioB bioB moaA moaA ygiQ ygiQ yjjW yjjW nrdG nrdG epmB epmB thiH thiH pflC pflC hemN hemN aslB aslB yhcC yhcC yggW yggW queE queE rlmN rlmN ydeM ydeM pflA pflA rimO rimO
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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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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)
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)
ygiQRadical SAM superfamily protein. (739 aa)
yjjWPutative activating enzyme; Protein involved in anaerobic respiration and protein modification process; Belongs to the organic radical-activating enzymes family. (287 aa)
nrdGAnaerobic ribonucleoside-triphosphate reductase-activating protein; Activation of anaerobic ribonucleoside-triphosphate reductase 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. (154 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)
thiHTyrosine lyase, involved in thiamine-thiazole moiety synthesis; Catalyzes the radical-mediated cleavage of tyrosine to 2- iminoacetate and 4-cresol. (377 aa)
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)
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)
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)
yhcCPutative Fe-S oxidoreductase, Radical SAM superfamily protein; In vitro, can cleave S-adenosyl-L-methionine into methionine and 5'-deoxyadenosine (AdoH); Belongs to the radical SAM superfamily. (309 aa)
yggWHemN family putative oxidoreductase; Probably acts as a heme chaperone, transferring heme to the NarI subunit of the respiratory enzyme nitrate reductase; transfer may be stimulated by NADH. Binds one molecule of heme per monomer, possibly covalently. Heme binding is not affected by either [4Fe-4S] or S- adenosyl-L-methionine (SAM)-binding. Does not have coproporphyrinogen III dehydrogenase activity in vitro. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (Probable). (378 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)
rlmNDual specificity 23S rRNA m(2)A2503, tRNA m(2)A37 methyltransferase, SAM-dependent; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. Belongs to the radical SAM superfamily. RlmN family. (384 aa)
ydeMPutative enzyme; Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family. (385 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)
rimORibosomal protein S12 methylthiotransferase; Catalyzes the methylthiolation of the residue Asp-89 of ribosomal protein S12. (441 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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