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XGPT_SHIFL
ID   XGPT_SHIFL              Reviewed;         152 AA.
AC   P0A9M7; P00501;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=SF0286, S0307;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN41945.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP15832.1; -; Genomic_DNA.
DR   RefSeq; NP_706238.1; NC_004337.2.
DR   RefSeq; WP_001291990.1; NZ_WPGW01000070.1.
DR   AlphaFoldDB; P0A9M7; -.
DR   SMR; P0A9M7; -.
DR   STRING; 198214.SF0286; -.
DR   EnsemblBacteria; AAN41945; AAN41945; SF0286.
DR   EnsemblBacteria; AAP15832; AAP15832; S0307.
DR   GeneID; 1024293; -.
DR   GeneID; 66671444; -.
DR   KEGG; sfl:SF0286; -.
DR   KEGG; sfx:S0307; -.
DR   PATRIC; fig|198214.7.peg.327; -.
DR   HOGENOM; CLU_080904_3_0_6; -.
DR   OMA; FHRDCRA; -.
DR   OrthoDB; 1819460at2; -.
DR   UniPathway; UPA00602; UER00658.
DR   UniPathway; UPA00909; UER00887.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome; Transferase.
FT   CHAIN           1..152
FT                   /note="Xanthine-guanine phosphoribosyltransferase"
FT                   /id="PRO_0000139687"
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;  16971 MW;  F0AD813127E7200D CRC64;
     MSEKYIVTWD MLQIHARKLA SRLMPSEQWK GIIAVSRGGL VPGALLAREL GIRHVDTVCI
     SSYDHDNQRE LKVLKRAEGD GEGFIVIDDL VDTGGTAVAI REMYPKAHFV TIFAKPAGRP
     LVDDYVVDIP QDTWIEQPWD MGVVFVPPIS GR
 
 
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