(data stored in ACNUC10821 zone)

SWISSPROT: C8U1W9_ECO10

ID   C8U1W9_ECO10            Unreviewed;       152 AA.
AC   C8U1W9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903};
DE            EC=2.4.2.22 {ECO:0000256|HAMAP-Rule:MF_01903};
DE   AltName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903};
DE            Short=XGPRT {ECO:0000256|HAMAP-Rule:MF_01903};
GN   Name=gpt {ECO:0000256|HAMAP-Rule:MF_01903,
GN   ECO:0000313|EMBL:BAI29127.1};
GN   OrderedLocusNames=ECO103_0253 {ECO:0000313|EMBL:BAI29127.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29127.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29127.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Acts on guanine, xanthine and to a lesser extent
CC       hypoxanthine. {ECO:0000256|HAMAP-Rule:MF_01903,
CC       ECO:0000256|SAAS:SAAS00724687}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58017;
CC         EC=2.4.2.22; Evidence={ECO:0000256|HAMAP-Rule:MF_01903,
CC         ECO:0000256|SAAS:SAAS01117944};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01903};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01903};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway;
CC       XMP from xanthine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01903,
CC       ECO:0000256|SAAS:SAAS00724688}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01903,
CC       ECO:0000256|SAAS:SAAS00724689}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01903}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01903}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. XGPT subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01903, ECO:0000256|SAAS:SAAS00724678}.
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DR   EMBL; AP010958; BAI29127.1; -; Genomic_DNA.
DR   RefSeq; WP_001291990.1; NC_013353.1.
DR   SMR; C8U1W9; -.
DR   EnsemblBacteria; BAI29127; BAI29127; ECO103_0253.
DR   KEGG; eoh:ECO103_0253; -.
DR   HOGENOM; HOG000226805; -.
DR   KO; K00769; -.
DR   OMA; FHRDCRA; -.
DR   BioCyc; ECOL585395:ECO103_RS01330-MONOMER; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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   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.
PE   3: Inferred from homology;
DR   PRODOM; C8U1W9.
DR   SWISS-2DPAGE; C8U1W9.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01903};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00724692};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00724681, ECO:0000313|EMBL:BAI29127.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00724684};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00724702};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00724691};
KW   Purine salvage {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00724693};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00724670, ECO:0000313|EMBL:BAI29127.1}.
FT   DOMAIN       11    144       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
FT   REGION       37     38       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01903}.
FT   REGION       92     96       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01903}.
FT   METAL        89     89       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01903}.
FT   BINDING      69     69       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01903}.
FT   BINDING      92     92       Xanthine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01903}.
FT   BINDING     135    135       Xanthine; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                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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