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deoD deoD upp upp AMM95107.1 AMM95107.1 AMM95099.1 AMM95099.1 hisZ hisZ hisG hisG AMM94047.1 AMM94047.1 tgt tgt apt apt purF_2 purF_2 pupG pupG deoA deoA xpt xpt murG2 murG2 glgB glgB glgA glgA yueK yueK pyrE pyrE pyrR pyrR trpD trpD cobT cobT purF_1 purF_1 hprT hprT
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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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deoDPurine nucleoside phosphorylase DeoD-type; Derived by automated computational analysis using gene prediction method: Protein Homology. (234 aa)
uppUracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. (209 aa)
AMM95107.1acetylglucosaminyldiphospho-UDP acetyl-beta-D-mannosaminyltransferase; Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid. (247 aa)
AMM95099.1Phosphoribosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (230 aa)
hisZATP phosphoribosyltransferase; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. (395 aa)
hisGATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Short subfamily. (209 aa)
AMM94047.1Nicotinate-nucleotide pyrophosphorylase; Catalyzes the formation of pyridine-2,3-dicarboxylate and 5-phospho-alpha-D-ribose 1-diphosphate from nictinate D-ribonucleotide; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the NadC/ModD family. (283 aa)
tgtQueuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] (379 aa)
aptAdenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. (170 aa)
purF_2Amidophosphoribosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (456 aa)
pupGPurine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. (270 aa)
deoAThymidine phosphorylase; Catalyzes the reversible phosphorolysis of thymidine, deoxyuridine and their analogues to their respective bases and 2-deoxyribose 1-phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology. (434 aa)
xptXanthine phosphoribosyltransferase; Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. (199 aa)
murG2UDP-diphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. (359 aa)
glgB1,4-alpha-glucan branching protein; Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position; Belongs to the glycosyl hydrolase 13 family. GlgB subfamily. (646 aa)
glgAGlycogen synthase; Synthesizes alpha-1,4-glucan chains using ADP-glucose. (478 aa)
yueKNicotinate phosphoribosyltransferase; Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Belongs to the NAPRTase family. (489 aa)
pyrEOrotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). (211 aa)
pyrRBifunctional pyrimidine regulatory protein PyrR uracil phosphoribosyltransferase; Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant; Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily. (181 aa)
trpDAnthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). (340 aa)
cobTNicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). (348 aa)
purF_1Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (471 aa)
hprTHypoxanthine phosphoribosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the purine/pyrimidine phosphoribosyltransferase family. (179 aa)
Your Current Organism:
Bacillus simplex
NCBI taxonomy Id: 1478
Other names: ATCC 49097, Arthrobacter sp. CHR2P1B2-M, B. simplex, Bacillus maroccanus, Bacillus sp. JP44SK12, Bacillus sp. JP44SK13, Bacillus sp. JP44SK25, Bacillus sp. JP44SK26, Bacillus sp. JP44SK29, Bacillus sp. JP44SK30, Bacillus sp. JP44SK31, Bacillus sp. JP44SK32, CCUG 28889, CIP 106934, IFO 15720, JCM 12307, LMG 11160, LMG:11160, NBRC 15720, NRRL NRS-960
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