ID A0A177PHS5_9HYPH Unreviewed; 161 AA. AC A0A177PHS5; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 29-MAY-2024, entry version 28. 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=A1351_01280 {ECO:0000313|EMBL:OAI29721.1}; OS Methylosinus sp. R-45379. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Methylocystaceae; Methylosinus. OX NCBI_TaxID=980563 {ECO:0000313|EMBL:OAI29721.1, ECO:0000313|Proteomes:UP000078138}; RN [1] {ECO:0000313|EMBL:OAI29721.1, ECO:0000313|Proteomes:UP000078138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R-45379 {ECO:0000313|EMBL:OAI29721.1, RC ECO:0000313|Proteomes:UP000078138}; RA Ploux O.; RL Submitted (MAR-2016) 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:OAI29721.1}. 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; LUUM01000223; OAI29721.1; -; Genomic_DNA. DR RefSeq; WP_024878890.1; NZ_LUUM01000223.1. DR AlphaFoldDB; A0A177PHS5; -. DR OrthoDB; 9789690at2; -. DR UniPathway; UPA00602; UER00658. DR UniPathway; UPA00909; UER00887. DR Proteomes; UP000078138; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0032264; P:IMP salvage; IEA:TreeGrafter. 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. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01903}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_01903}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01903}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01903}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01903}; KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP- KW Rule:MF_01903}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01903}. FT DOMAIN 10..152 FT /note="Phosphoribosyltransferase" FT /evidence="ECO:0000259|Pfam:PF00156" FT BINDING 38..39 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 95..103 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 96 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 99..103 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 99 FT /ligand="guanine" FT /ligand_id="ChEBI:CHEBI:16235" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 99 FT /ligand="xanthine" FT /ligand_id="ChEBI:CHEBI:17712" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 141..142 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 142 FT /ligand="guanine" FT /ligand_id="ChEBI:CHEBI:16235" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 142 FT /ligand="xanthine" FT /ligand_id="ChEBI:CHEBI:17712" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" SQ SEQUENCE 161 AA; 17508 MW; 4F4857B4CE71C1FB CRC64; MEDKAFPVSW DAFHRDARAL AWRLSAVGGF SAIVAVTRGG LVPAGVVARE LGIRVIDTIG VASYQEETQR GEVRVLKPLS ETILTLPSEE VLIVDDLVDT GATAKVVRAL LPNAHFATVY AKPQGRPLVD TFVTEVSQDT WIFFPWDTGL SFQAPIARES S //