ID A0A177PHS5_9RHIZ Unreviewed; 161 AA. AC A0A177PHS5; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 22-NOV-2017, entry version 9. DE RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903}; DE EC=2.4.2.22 {ECO:0000256|HAMAP-Rule:MF_01903}; DE AltName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903}; DE Short=XGPRT {ECO:0000256|HAMAP-Rule:MF_01903}; GN Name=gpt {ECO:0000256|HAMAP-Rule:MF_01903}; GN ORFNames=A1351_01280 {ECO:0000313|EMBL:OAI29721.1}; OS Methylosinus sp. R-45379. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylocystaceae; Methylosinus. OX NCBI_TaxID=980563 {ECO:0000313|EMBL:OAI29721.1, ECO:0000313|Proteomes:UP000078138}; RN [1] {ECO:0000313|EMBL:OAI29721.1, ECO:0000313|Proteomes:UP000078138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R-45379 {ECO:0000313|EMBL:OAI29721.1, RC ECO:0000313|Proteomes:UP000078138}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Acts on guanine, xanthine and to a lesser extent CC hypoxanthine. {ECO:0000256|HAMAP-Rule:MF_01903, CC ECO:0000256|SAAS:SAAS00724687}. CC -!- CATALYTIC ACTIVITY: XMP + diphosphate = 5-phospho-alpha-D-ribose CC 1-diphosphate + xanthine. {ECO:0000256|HAMAP-Rule:MF_01903, CC ECO:0000256|SAAS:SAAS00724699}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01903}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01903}; CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; CC XMP from xanthine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01903, CC ECO:0000256|SAAS:SAAS00724688}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01903, CC ECO:0000256|SAAS:SAAS00724689}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01903}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01903}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. XGPT subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01903, ECO:0000256|SAAS:SAAS00724678}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01903}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAI29721.1}. 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; LUUM01000223; OAI29721.1; -; Genomic_DNA. DR RefSeq; WP_024878890.1; NZ_LUUM01000223.1. DR EnsemblBacteria; OAI29721; OAI29721; A1351_01280. DR UniPathway; UPA00602; UER00658. DR Proteomes; UP000078138; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule. DR GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway. DR CDD; cd06223; PRTases_typeI; 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. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000256|SAAS:SAAS00724692}; KW Complete proteome {ECO:0000313|Proteomes:UP000078138}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000256|SAAS:SAAS00724681, ECO:0000313|EMBL:OAI29721.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000256|SAAS:SAAS00724684}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000256|SAAS:SAAS00724702}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000256|SAAS:SAAS00724691}; KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000256|SAAS:SAAS00724693}; KW Reference proteome {ECO:0000313|Proteomes:UP000078138}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000256|SAAS:SAAS00724670, ECO:0000313|EMBL:OAI29721.1}. FT DOMAIN 13 152 Pribosyltran. {ECO:0000259|Pfam:PF00156}. FT REGION 38 39 5-phosphoribose 1-diphosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01903}. FT REGION 99 103 5-phosphoribose 1-diphosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01903}. FT METAL 96 96 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01903}. FT BINDING 99 99 Xanthine. {ECO:0000256|HAMAP-Rule: FT MF_01903}. FT BINDING 142 142 Xanthine; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01903}. SQ SEQUENCE 161 AA; 17508 MW; 4F4857B4CE71C1FB CRC64; MEDKAFPVSW DAFHRDARAL AWRLSAVGGF SAIVAVTRGG LVPAGVVARE LGIRVIDTIG VASYQEETQR GEVRVLKPLS ETILTLPSEE VLIVDDLVDT GATAKVVRAL LPNAHFATVY AKPQGRPLVD TFVTEVSQDT WIFFPWDTGL SFQAPIARES S //