(data stored in ACNUC7421 zone)

SWISSPROT: XGPT_SALTY

ID   XGPT_SALTY              Reviewed;         152 AA.
AC   P0A277; P26972;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903};
DE            EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01903};
DE   AltName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903};
DE            Short=XGPRT {ECO:0000255|HAMAP-Rule:MF_01903};
GN   Name=gpt {ECO:0000255|HAMAP-Rule:MF_01903}; OrderedLocusNames=STM0317;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RA   Bryant D.W., Rossetto F.E., O'Reilly C., Nieboer E., Turnbull J.;
RL   Submitted (NOV-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29631 / TA 1538;
RX   PubMed=8962426; DOI=10.1093/mutage/11.6.565;
RA   Matsui M., Sofuni T., Nohmi T.;
RT   "Regionally-targeted mutagenesis by metabolically-activated steviol: DNA
RT   sequence analysis of steviol-induced mutants of guanine
RT   phosphoribosyltransferase (gpt) gene of Salmonella typhimurium TM677.";
RL   Mutagenesis 11:565-572(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Acts on guanine, xanthine and to a lesser extent
CC       hypoxanthine.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01903};
CC       Note=Binds 1 Mg(2+) ion per subunit. {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}.
DR   EMBL; X63336; CAA44936.1; -; Genomic_DNA.
DR   EMBL; U28239; AAC01774.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19273.1; -; Genomic_DNA.
DR   PIR; S18888; S18888.
DR   RefSeq; NP_459314.1; NC_003197.2.
DR   RefSeq; WP_001292018.1; NC_003197.2.
DR   SMR; P0A277; -.
DR   PaxDb; P0A277; -.
DR   PRIDE; P0A277; -.
DR   EnsemblBacteria; AAL19273; AAL19273; STM0317.
DR   GeneID; 1251836; -.
DR   KEGG; stm:STM0317; -.
DR   PATRIC; fig|99287.12.peg.337; -.
DR   eggNOG; ENOG4105DYA; Bacteria.
DR   eggNOG; COG0503; LUCA.
DR   HOGENOM; HOG000226805; -.
DR   KO; K00769; -.
DR   OMA; FHRDCRA; -.
DR   PhylomeDB; P0A277; -.
DR   BioCyc; SENT99287:STM0317-MONOMER; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0032263; P:GMP salvage; IBA:GO_Central.
DR   GO; GO:0032264; P:IMP salvage; IBA:GO_Central.
DR   GO; GO:0032265; P:XMP salvage; IBA:GO_Central.
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;
DR   PRODOM; P0A277.
DR   SWISS-2DPAGE; P0A277.
KW   Cell inner membrane; Cell membrane; Glycosyltransferase; Magnesium;
KW   Membrane; Metal-binding; Purine salvage; Reference proteome; Transferase.
FT   CHAIN           1..152
FT                   /note="Xanthine phosphoribosyltransferase"
FT                   /id="PRO_0000139686"
FT   REGION          37..38
FT                   /note="5-phosphoribose 1-diphosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   REGION          92..96
FT                   /note="5-phosphoribose 1-diphosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   METAL           89
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   BINDING         69
FT                   /note="5-phosphoribose 1-diphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   BINDING         92
FT                   /note="Xanthine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   BINDING         135
FT                   /note="Xanthine; via amide nitrogen and carbonyl oxygen"
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
//

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