(data stored in SCRATCH zone)

SWISSPROT: C8U1J5_ECO10

ID   C8U1J5_ECO10            Unreviewed;       178 AA.
AC   C8U1J5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 46.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE            EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN   Name=hpt {ECO:0000313|EMBL:BAI29003.1};
GN   OrderedLocusNames=ECO103_0125 {ECO:0000313|EMBL:BAI29003.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29003.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29003.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973,
CC         ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:58053; EC=2.4.2.8;
CC         Evidence={ECO:0000256|RuleBase:RU364099};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364099};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC       IMP from hypoxanthine: step 1/1. {ECO:0000256|RuleBase:RU364099}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364099}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|RuleBase:RU364099}.
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DR   EMBL; AP010958; BAI29003.1; -; Genomic_DNA.
DR   RefSeq; WP_000683335.1; NC_013353.1.
DR   SMR; C8U1J5; -.
DR   EnsemblBacteria; BAI29003; BAI29003; ECO103_0125.
DR   KEGG; eoh:ECO103_0125; -.
DR   HOGENOM; HOG000236520; -.
DR   KO; K00760; -.
DR   OMA; TMDWMAV; -.
DR   BioCyc; ECOL585395:ECO103_RS00640-MONOMER; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01203; HGPRTase; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1J5.
DR   SWISS-2DPAGE; C8U1J5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364099};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU364099,
KW   ECO:0000313|EMBL:BAI29003.1};
KW   Magnesium {ECO:0000256|RuleBase:RU364099};
KW   Metal-binding {ECO:0000256|RuleBase:RU364099};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364099};
KW   Purine salvage {ECO:0000256|RuleBase:RU364099};
KW   Transferase {ECO:0000256|RuleBase:RU364099,
KW   ECO:0000313|EMBL:BAI29003.1}.
FT   DOMAIN       13    160       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
SQ   SEQUENCE   178 AA;  20115 MW;  E1A75EB68231DC32 CRC64;
     MKHTVEVMIP EAEIKARIAE LGRQITERYK DSGSDMVLVG LLRGSFMFMA DLCREVQVSH
     EVDFMTASSY GSGMSTTRDV KILKDLDEDI RGKDVLIVED IIDSGNTLSK VREILSLREP
     KSLAICTLLD KPSRREVNVP VEFIGFSIPD EFVVGYGIDY AQRYRHLPYI GKVILLDE
//

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