XGPT_SALNS
ID XGPT_SALNS Reviewed; 152 AA.
AC B4SVV9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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};
GN OrderedLocusNames=SNSL254_A0356;
OS Salmonella newport (strain SL254).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=423368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL254;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(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}.
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DR EMBL; CP001113; ACF63568.1; -; Genomic_DNA.
DR RefSeq; WP_001292018.1; NZ_CCMR01000003.1.
DR AlphaFoldDB; B4SVV9; -.
DR SMR; B4SVV9; -.
DR EnsemblBacteria; ACF63568; ACF63568; SNSL254_A0356.
DR GeneID; 66754798; -.
DR KEGG; see:SNSL254_A0356; -.
DR HOGENOM; CLU_080904_3_0_6; -.
DR OMA; FHRDCRA; -.
DR UniPathway; UPA00602; UER00658.
DR UniPathway; UPA00909; UER00887.
DR Proteomes; UP000008824; 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; Transferase.
FT CHAIN 1..152
FT /note="Xanthine-guanine phosphoribosyltransferase"
FT /id="PRO_1000188757"
FT BINDING 37..38
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 69
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 69
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 88..96
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 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 92..96
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 92
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 92
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 134..135
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 135
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 135
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
SQ SEQUENCE 152 AA; 16970 MW; EE42974303E6900D CRC64;
MSEKYVVTWD MLQIHARKLA SRLMPSEQWK GIIAVSRGGL VPGALLAREL GIRHVDTVCI
SSYDHDNQRE LKVLKRAEGD GEGFIVIDDL VDTGGTAVAI REMYPKAHFV TIFAKPAGRP
LVDDYVIDIP QNTWIEQPWD MGVVFVPPIS GR
