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XGPT_SODGM
ID   XGPT_SODGM              Reviewed;         152 AA.
AC   Q2NVF2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, 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=SG0598;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE73873.1; -; Genomic_DNA.
DR   RefSeq; WP_011410351.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NVF2; -.
DR   SMR; Q2NVF2; -.
DR   STRING; 343509.SG0598; -.
DR   EnsemblBacteria; BAE73873; BAE73873; SG0598.
DR   KEGG; sgl:SG0598; -.
DR   eggNOG; COG2236; Bacteria.
DR   HOGENOM; CLU_080904_3_0_6; -.
DR   OMA; FHRDCRA; -.
DR   OrthoDB; 1819460at2; -.
DR   BioCyc; SGLO343509:SGP1_RS05140-MON; -.
DR   UniPathway; UPA00602; UER00658.
DR   UniPathway; UPA00909; UER00887.
DR   Proteomes; UP000001932; 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_0000261022"
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;  16912 MW;  EBEB92DB1F7F65F0 CRC64;
     MSEKYVVTWD MLQIHARTMA KLLLPAEQWK GIIAVSRGGL VPGALLAREL GIRHVDTVCI
     ASYDHDNQRD LNVLKRAEAD GEGFIVVDDL VDTGVTAKAI REMYPKAHFV TIFAKPAGRP
     LVDDYIIDIP QNTWIEQPWD MGVVFVSPLA GK
 
 
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