ID A0AA50Q6T2_9GAMM Unreviewed; 156 AA. AC A0AA50Q6T2; DT 24-JAN-2024, integrated into UniProtKB/TrEMBL. DT 24-JAN-2024, sequence version 1. DT 24-JUL-2024, entry version 4. 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 ECO:0000313|EMBL:WMC09745.1}; GN ORFNames=PU634_11545 {ECO:0000313|EMBL:WMC09745.1}; OS Oceanimonas pelagia. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Oceanimonas. OX NCBI_TaxID=3028314 {ECO:0000313|EMBL:WMC09745.1}; RN [1] {ECO:0000313|EMBL:WMC09745.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NTOU-MSR1 {ECO:0000313|EMBL:WMC09745.1}; RA Yang H.-T., Chen Y.-L., Ho Y.-N.; RT "Complete genome sequence of a novel bacterium Oceanimonas sp. NTOU-MSR1 RT isolated from marine coast sediment."; RL Submitted (FEB-2023) 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 --------------------------------------------------------------------------- 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; CP118224; WMC09745.1; -; Genomic_DNA. DR KEGG; ope:PU634_11545; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:TreeGrafter. 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:TreeGrafter. 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:TreeGrafter. 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 15..144 FT /note="Phosphoribosyltransferase" FT /evidence="ECO:0000259|Pfam:PF00156" FT BINDING 37..38 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 89..97 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 90 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 93..97 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 93 FT /ligand="guanine" FT /ligand_id="ChEBI:CHEBI:16235" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 93 FT /ligand="xanthine" FT /ligand_id="ChEBI:CHEBI:17712" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 135..136 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 136 FT /ligand="guanine" FT /ligand_id="ChEBI:CHEBI:16235" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" FT BINDING 136 FT /ligand="xanthine" FT /ligand_id="ChEBI:CHEBI:17712" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903" SQ SEQUENCE 156 AA; 17553 MW; B70E1A1B4A27FFE0 CRC64; MSNKFVVTWD SFQREARKLA ARQLPASQWK GIIAVSRGGL VPAAILAREL GIRHVDTLCI SSYDHNQQRD DLQVLKQVNG DGEGFLIVDD LVDTGNTARV IRELYPKAKF ITVFAKPKGE PLVDDFEVRV GQDTWIEQPW DMSVTFVPPL CEQDQA //