ID XGPT_BUCAI Reviewed; 158 AA. AC P57339; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 24-JAN-2024, entry version 124. 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=BU251; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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 -!- SEQUENCE CAUTION: CC Sequence=BAB12961.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; BA000003; BAB12961.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_240075.2; NC_002528.1. DR RefSeq; WP_009874205.1; NC_002528.1. DR AlphaFoldDB; P57339; -. DR SMR; P57339; -. DR STRING; 563178.BUAP5A_246; -. DR EnsemblBacteria; BAB12961; BAB12961; BAB12961. DR KEGG; buc:BU251; -. DR PATRIC; fig|107806.10.peg.261; -. DR eggNOG; COG2236; Bacteria. DR HOGENOM; CLU_080904_3_0_6; -. DR OMA; FHRDCRA; -. DR UniPathway; UPA00602; UER00658. DR UniPathway; UPA00909; UER00887. DR Proteomes; UP000001806; 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; XANTHINE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR39563:SF1; XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; PRTase-like; 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..158 FT /note="Xanthine-guanine phosphoribosyltransferase" FT /id="PRO_0000139660" FT BINDING 38..39 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 90..98 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 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 94..98 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 94 FT /ligand="guanine" FT /ligand_id="ChEBI:CHEBI:16235" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 94 FT /ligand="xanthine" FT /ligand_id="ChEBI:CHEBI:17712" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 136..137 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 137 FT /ligand="guanine" FT /ligand_id="ChEBI:CHEBI:16235" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" FT BINDING 137 FT /ligand="xanthine" FT /ligand_id="ChEBI:CHEBI:17712" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903" SQ SEQUENCE 158 AA; 18064 MW; 2B40B2A98EAABF28 CRC64; MSEKYIVTWD MLQIHTRKLA NRLVKKIHSW NGIIAVSRGG LVPSALLARE LGLRCVDTVC IESYNYDCLK ENRKIIKKAE GNGEKIIVID DLVDTGGTAK IIRKLYPKAC FVTIFAKPMG RSLVDNYIID IPQNVWIEQP WDMSISYIPP LIQNYKIK //