ID A0A4Q3ZFS6_9RHOB Unreviewed; 167 AA. AC A0A4Q3ZFS6; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 16-OCT-2019, entry version 3. 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=EU800_09795 {ECO:0000313|EMBL:RYH10167.1}; OS Tropicimonas sp. IMCC6043. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Tropicimonas. OX NCBI_TaxID=2510645 {ECO:0000313|EMBL:RYH10167.1, ECO:0000313|Proteomes:UP000293926}; RN [1] {ECO:0000313|EMBL:RYH10167.1, ECO:0000313|Proteomes:UP000293926} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC6043 {ECO:0000313|EMBL:RYH10167.1, RC ECO:0000313|Proteomes:UP000293926}; RA Jang H.-J.; RT "Tropicimonas IMCC6043, genome."; RL Submitted (FEB-2019) 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: CC Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1- CC diphosphate + xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58017; CC EC=2.4.2.22; Evidence={ECO:0000256|HAMAP-Rule:MF_01903, CC ECO:0000256|SAAS:SAAS01117944}; 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:RYH10167.1}. 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; SELO01000007; RYH10167.1; -; Genomic_DNA. DR UniPathway; UPA00602; UER00658. DR Proteomes; UP000293926; 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 PANTHER; PTHR39563; PTHR39563; 1. 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:UP000293926}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000256|SAAS:SAAS00724681, ECO:0000313|EMBL:RYH10167.1}; 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:UP000293926}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000256|SAAS:SAAS00724670, ECO:0000313|EMBL:RYH10167.1}. FT DOMAIN 15 159 Pribosyltran. {ECO:0000259|Pfam:PF00156}. FT REGION 47 48 5-phosphoribose 1-diphosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01903}. FT REGION 106 110 5-phosphoribose 1-diphosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01903}. FT METAL 103 103 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01903}. FT BINDING 106 106 Xanthine. {ECO:0000256|HAMAP-Rule: FT MF_01903}. FT BINDING 149 149 Xanthine; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01903}. SQ SEQUENCE 167 AA; 18910 MW; 11F17B1087B1A8D3 CRC64; MSDRLPHEKG FHISWDQIHR DSRALAWRLD GHGPLDGGWK AIVAITRGGM APAMIIAREL DVRTVDTISV KSYNHQHQTD AKVLKAPDVE MMGDGTGILI IDDLVDSGKT LELVRKMYPK AHFATVYAKP KGRPMVDTYI TEVSQDTWIF FPWDMALQYV EPYRGTD //