ID XGPT_BUCAI Reviewed; 158 AA. AC P57339; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 05-OCT-2016, entry version 99. 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}; OrderedLocusNames=BU251; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OS (Acyrthosiphon pisum symbiotic bacterium). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids RT Buchnera sp. APS."; RL Nature 407:81-86(2000). 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 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 -!- SEQUENCE CAUTION: CC Sequence=BAB12961.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; BA000003; BAB12961.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_240075.2; NC_002528.1. DR RefSeq; WP_009874205.1; NC_002528.1. DR ProteinModelPortal; P57339; -. DR STRING; 107806.BU251; -. DR EnsemblBacteria; BAB12961; BAB12961; BAB12961. DR GeneID; 1109690; -. DR KEGG; buc:BU251; -. DR PATRIC; 21244026; VBIBucAph127364_0261. DR eggNOG; ENOG4105DYA; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000226805; -. DR KO; K00769; -. DR OMA; FHRDCRA; -. DR BioCyc; BAPH107806:GBZJ-251-MONOMER; -. DR UniPathway; UPA00602; UER00658. DR Proteomes; UP000001806; 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 CDD; cd06223; PRTases_typeI; 1. 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 membrane; Complete proteome; Glycosyltransferase; Magnesium; KW Membrane; Metal-binding; Purine salvage; Reference proteome; KW Transferase. FT CHAIN 1 158 Xanthine phosphoribosyltransferase. FT /FTId=PRO_0000139660. FT REGION 38 39 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01903}. FT REGION 94 98 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01903}. FT METAL 91 91 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01903}. FT BINDING 94 94 Xanthine. {ECO:0000255|HAMAP- FT Rule:MF_01903}. FT BINDING 137 137 Xanthine; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01903}. SQ SEQUENCE 158 AA; 18064 MW; 2B40B2A98EAABF28 CRC64; MSEKYIVTWD MLQIHTRKLA NRLVKKIHSW NGIIAVSRGG LVPSALLARE LGLRCVDTVC IESYNYDCLK ENRKIIKKAE GNGEKIIVID DLVDTGGTAK IIRKLYPKAC FVTIFAKPMG RSLVDNYIID IPQNVWIEQP WDMSISYIPP LIQNYKIK //