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dck dck dgk dgk tilS tilS hprT hprT yerA yerA yfkN yfkN guaD guaD adeC adeC deoD deoD pupG pupG cdd cdd udk udk apt apt pucH pucH pucR pucR pucJ pucJ pucL pucL pucM pucM pucE pucE pucD pucD pucC pucC pucB pucB pucA pucA pucG pucG pucF pucF pucI pucI upp upp pdp pdp
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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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experimentally determined
Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
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Your Input:
dckDeoxyadenosine/deoxycytidine kinase; Plays an essential role in generating the deoxyribonucleotide precursors dATP AND dCTP for DNA metabolism. The phosphate acceptor specificity is strict toward deoxyadenosine (dAdo) and deoxycytidine (dCyd). The specificity toward the sugar moiety of the nucleoside is less strict. Both 2-deoxyribose, ribose, and arabinose nucleosides are phosphorylated, although the 2-deoxyribonucleosides are preferred. The phosphate donor specificity is dependent on the deoxyribonucleoside substrate, but GTP is efficient with both deoxycytidine and deoxyadenosine. O [...] (217 aa)
dgkDeoxyguanosine kinase; Plays an essential role in generating the deoxyribonucleotide precursors dGTP for DNA metabolism. Highly specific toward deoxyguanosine (dGuo) and deoxyinosine (dIno). Only marginal activity is observed with guanosine. UTP is slightly more efficient as phosphate donor than CTP, ATP and GTP. (207 aa)
tilStRNAile lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. (472 aa)
hprTHypoxanthine-guanine phosphoribosyltransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (180 aa)
yerAPutative adenine deaminase YerA; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (580 aa)
yfkNExported 2',3'-cyclic-nucleotide 2'-phosphodiesterase, 2' (or 3') nucleotidase and 5' nucleotidase; Catalyzes the release of inorganic phosphate from 2',3'- cyclic nucleotides through consecutive 2',3'-phosphodiesterase and 3'- (or 2') nucleotidase activities. Also possesses a 5'-nucleotidase activity. Does not catalyze the release of inorganic phosphate from 3',5'-cyclic nucleotides. Probably plays a role in the cellular reprocessing of nucleotides present in the medium, under conditions of phosphate shortage. (1462 aa)
guaDGuanine deaminase; Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. (156 aa)
adeCAdenine deaminase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family. (577 aa)
deoDPurine nucleoside phosphorylase; Cleavage of adenosine and its derivatives; Belongs to the PNP/UDP phosphorylase family. (233 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. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine. (271 aa)
cddCytidine/deoxycytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. (136 aa)
udkUridine kinase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme. (211 aa)
aptAdenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. (170 aa)
pucHAllantoinase; Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. (446 aa)
pucRTranscriptional regulator of the purine degradation operon; Activates the expression of pucFG, pucH, pucI, pucJKLM and guaD, while it represses pucABCDE and its own expression. Belongs to the CdaR family. (531 aa)
pucJUric acid permease; Uptake of uric acid. (449 aa)
pucLUrate oxidase with peroxide reductase N-terminal domain; Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5- ureidoimidazoline (OHCU) to (S)-allantoin. (494 aa)
pucM5-hydroxyisourate hydrolase; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). (114 aa)
pucEXanthine dehydrogenase, iron-sulfur subunit; Oxidizes hypoxanthine and xanthine to uric acid. (173 aa)
pucDXanthine dehydrogenase, substrate and molybdenum cofactor subunit; Oxidizes hypoxanthine and xanthine to uric acid. Belongs to the xanthine dehydrogenase family. (745 aa)
pucCXanthine dehydrogenase, FAD-binding subunit; Oxidizes hypoxanthine and xanthine to uric acid. (277 aa)
pucBEnzyme for molybdopterin cofactor synthesis required for xanthine dehydrogenase; Required for xanthine dehydrogenase activity. Could be involved in formation of the molybdenum cofactor required by xanthine dehydrogenase. (205 aa)
pucAXanthine dehydrogenase molybdopterin recruitment factor; Oxidizes hypoxanthine and xanthine to uric acid. PucA subunit could exert a molybdenum cofactor recruiting function. (330 aa)
pucGVitamin B6-dependent (S)-ureidoglycine glyoxylate aminotransferase; Catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the preferred substrate, but other amino-group acceptors can be used. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. (416 aa)
pucFAllantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S- ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (By similarity). (412 aa)
pucIAllantoin permease; Transport of allantoin. (490 aa)
uppUracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. (209 aa)
pdpPyrimidine-nucleoside phosphorylase; Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate. (433 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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