ID XGPT_OLEA2 Reviewed; 162 AA. AC Q311U1; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 12-OCT-2022, entry version 102. DE RecName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903}; DE Short=XGPRT {ECO:0000255|HAMAP-Rule:MF_01903}; DE EC=2.4.2.- {ECO:0000255|HAMAP-Rule:MF_01903}; DE EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01903}; DE AltName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903}; GN Name=gpt {ECO:0000255|HAMAP-Rule:MF_01903}; OrderedLocusNames=Dde_1506; OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) OS (Desulfovibrio alaskensis). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Oleidesulfovibrio. OX NCBI_TaxID=207559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1058 / DSM 17464 / 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., Tapia R., RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., RA 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: 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:0000255|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:0000255|HAMAP- CC Rule:MF_01903}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426; CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01903}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10802; CC Evidence={ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_01903}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975; CC Evidence={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 -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP CC from guanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01903}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP CC 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 phosphoribosyltransferase CC family. XGPT subfamily. {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 AlphaFoldDB; Q311U1; -. DR SMR; Q311U1; -. DR STRING; 207559.Dde_1506; -. DR EnsemblBacteria; ABB38305; ABB38305; Dde_1506. DR KEGG; dde:Dde_1506; -. DR eggNOG; COG2236; Bacteria. DR HOGENOM; CLU_080904_3_0_7; -. DR OMA; FHRDCRA; -. DR OrthoDB; 1819460at2; -. DR UniPathway; UPA00602; UER00658. DR UniPathway; UPA00909; UER00887. DR Proteomes; UP000002710; Chromosome. 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. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Glycosyltransferase; Magnesium; KW Membrane; Metal-binding; Purine salvage; Reference proteome; Transferase. FT CHAIN 1..162 FT /note="Xanthine-guanine phosphoribosyltransferase" FT /id="PRO_0000261005" FT BINDING 43..44 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 94..102 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 95 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 98..102 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 98 FT /ligand="guanine" FT /ligand_id="ChEBI:CHEBI:16235" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 98 FT /ligand="xanthine" FT /ligand_id="ChEBI:CHEBI:17712" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 140..141 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 141 FT /ligand="guanine" FT /ligand_id="ChEBI:CHEBI:16235" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 141 FT /ligand="xanthine" FT /ligand_id="ChEBI:CHEBI:17712" FT /evidence="ECO:0000255|HAMAP-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 //