ID A0A4Q3ZFS6_9RHOB Unreviewed; 167 AA. AC A0A4Q3ZFS6; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 29-SEP-2021, entry version 10. DE RecName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903}; DE Short=XGPRT {ECO:0000256|HAMAP-Rule:MF_01903}; DE EC=2.4.2.22 {ECO:0000256|HAMAP-Rule:MF_01903}; DE AltName: Full=Xanthine phosphoribosyltransferase {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; unclassified 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: Purine salvage pathway enzyme that catalyzes the transfer of CC the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1- CC diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and CC xanthine to form the corresponding ribonucleotides GMP (guanosine 5'- CC monophosphate) and XMP (xanthosine 5'-monophosphate), with the release CC of PPi. To a lesser extent, also acts on hypoxanthine. CC {ECO:0000256|HAMAP-Rule:MF_01903}. CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate + CC guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01903}; CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + CC hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01903}; CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate + CC xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57464, ChEBI:CHEBI:58017; EC=2.4.2.22; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01903}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01903}; CC -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP CC from guanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01903}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP CC from xanthine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01903}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01903}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01903}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01903}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase CC family. XGPT subfamily. {ECO:0000256|HAMAP-Rule:MF_01903}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01903}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 UniPathway; UPA00909; UER00887. DR Proteomes; UP000293926; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:RHEA. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:RHEA. 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:0032263; P:GMP salvage; IEA:UniProtKB-UniPathway. 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 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 PANTHER; PTHR39563; PTHR39563; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01903}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903, KW ECO:0000313|EMBL:RYH10167.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01903}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01903}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01903}; KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP- KW Rule:MF_01903}; Reference proteome {ECO:0000313|Proteomes:UP000293926}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01903}. FT DOMAIN 15..159 FT /note="Pribosyltran" FT /evidence="ECO:0000259|Pfam:PF00156" FT NP_BIND 106..110 FT /note="GMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT NP_BIND 148..149 FT /note="GMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT REGION 47..48 FT /note="5-phospho-alpha-D-ribose 1-diphosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT REGION 102..110 FT /note="5-phospho-alpha-D-ribose 1-diphosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT METAL 103 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 106 FT /note="Xanthine or guanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 149 FT /note="Xanthine or guanine; via amide nitrogen and carbonyl FT oxygen" FT /evidence="ECO:0000256|HAMAP-Rule: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 //