ID XGPT_DESAG Reviewed; 162 AA. AC Q311U1; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 16-SEP-2015, entry version 73. DE RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903}; DE EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01903}; DE AltName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903}; DE Short=XGPRT {ECO:0000255|HAMAP-Rule:MF_01903}; GN Name=gpt {ECO:0000255|HAMAP-Rule:MF_01903}; GN OrderedLocusNames=Dde_1506; OS Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans OS (strain G20)). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=207559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G20; RX PubMed=21685289; DOI=10.1128/JB.05400-11; RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., RA Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., RA Lucas S., Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.; RT "Complete genome sequence and updated annotation of Desulfovibrio RT alaskensis G20."; RL J. Bacteriol. 193:4268-4269(2011). CC -!- FUNCTION: Acts on guanine, xanthine and to a lesser extent CC hypoxanthine. {ECO:0000255|HAMAP-Rule:MF_01903}. CC -!- CATALYTIC ACTIVITY: XMP + diphosphate = 5-phospho-alpha-D-ribose CC 1-diphosphate + xanthine. {ECO:0000255|HAMAP-Rule:MF_01903}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01903}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01903}; CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; CC XMP from xanthine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01903}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01903}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01903}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01903}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. XGPT subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01903}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000112; ABB38305.1; -; Genomic_DNA. DR RefSeq; WP_011367470.1; NC_007519.1. DR ProteinModelPortal; Q311U1; -. DR STRING; 207559.Dde_1506; -. DR EnsemblBacteria; ABB38305; ABB38305; Dde_1506. DR KEGG; dde:Dde_1506; -. DR PATRIC; 21741953; VBIDesDes50040_1499. DR eggNOG; COG0503; -. DR HOGENOM; HOG000226805; -. DR KO; K00769; -. DR OrthoDB; EOG6H1Q23; -. DR BioCyc; DALA207559:GH1L-1309-MONOMER; -. DR UniPathway; UPA00602; UER00658. DR Proteomes; UP000002710; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01903; XGPRT; 1. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR023747; Xanthine_Guanine_PRibTrfase. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Glycosyltransferase; Magnesium; Membrane; Metal-binding; KW Purine salvage; Reference proteome; Transferase. FT CHAIN 1 162 Xanthine phosphoribosyltransferase. FT /FTId=PRO_0000261005. FT REGION 43 44 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01903}. FT REGION 98 102 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01903}. FT METAL 95 95 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01903}. FT BINDING 98 98 Xanthine. {ECO:0000255|HAMAP- FT Rule:MF_01903}. FT BINDING 141 141 Xanthine; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01903}. SQ SEQUENCE 162 AA; 18276 MW; 43E478F3FDAE31EC CRC64; MADPDRYNKM FPVSWEQLHR DTRALSWRLM ERGPFKGIVA ITRGGLVPAA ILARELEVRL VDTICIASYD WKSQGGISVL KGVEGDGEGW LIVDDLVDTG TTARAVREML PKAHFATVYA KPSGRPVVDT YITEVSQDTW ILFPWDSEIQ YVQPLVNRRQ EG //