ID XGPT_DESAG Reviewed; 162 AA. AC Q311U1; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 02-DEC-2020, entry version 95. 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 Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans (strain OS G20)). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=207559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=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 SMR; Q311U1; -. DR STRING; 207559.Dde_1506; -. DR PRIDE; Q311U1; -. 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 BioCyc; DALA207559:G1G52-1386-MONOMER; -. 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: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: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 NP_BIND 98..102 FT /note="GMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT NP_BIND 140..141 FT /note="GMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT REGION 43..44 FT /note="5-phospho-alpha-D-ribose 1-diphosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT REGION 94..102 FT /note="5-phospho-alpha-D-ribose 1-diphosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT METAL 95 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 98 FT /note="Xanthine or guanine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 141 FT /note="Xanthine or guanine; via amide nitrogen and carbonyl FT oxygen" 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 //