(data stored in ACNUC10043 zone)

SWISSPROT: HPRT_METPS

ID   HPRT_METPS              Reviewed;         191 AA.
AC   D1YVK0;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 46.
DE   RecName: Full=Hypoxanthine/guanine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01467};
DE            Short=HGPRTase {ECO:0000255|HAMAP-Rule:MF_01467};
DE            EC=2.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01467};
GN   Name=hpt {ECO:0000255|HAMAP-Rule:MF_01467}; OrderedLocusNames=MCP_0400;
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE;
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC       IMP that is energically less costly than de novo synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01467}.
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; EC=2.4.2.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01467};
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; EC=2.4.2.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01467};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01467}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01467}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01467}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. Archaeal HPRT subfamily. {ECO:0000255|HAMAP-Rule:MF_01467}.
DR   EMBL; AP011532; BAI60472.1; -; Genomic_DNA.
DR   SMR; D1YVK0; -.
DR   STRING; 304371.MCP_0400; -.
DR   EnsemblBacteria; BAI60472; BAI60472; MCP_0400.
DR   KEGG; mpd:MCP_0400; -.
DR   PATRIC; fig|304371.9.peg.410; -.
DR   eggNOG; arCOG00030; Archaea.
DR   eggNOG; COG0503; LUCA.
DR   HOGENOM; HOG000228520; -.
DR   KO; K00759; -.
DR   OMA; FIHPISD; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000001882; 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-UniRule.
DR   GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-UniRule.
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   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_01467; Hypx_phosphoribosyltr; 1.
DR   InterPro; IPR026597; HGPRTase-like.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
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; D1YVK0.
DR   SWISS-2DPAGE; D1YVK0.
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN           1..191
FT                   /note="Hypoxanthine/guanine phosphoribosyltransferase"
FT                   /id="PRO_0000415470"
SQ   SEQUENCE   191 AA;  21024 MW;  181980EB9BCE46AE CRC64;
     MLKNLRETMR TAPIVRRGTY NYFIHPISDG VPVVKPELLR EVIACMVKNA DLDVDKIVTI
     EAMGLPLGAA LSTMTDIPFI IIRKRKYELP GEIAVHQTTG YSRGELYLNG INKGDRVLII
     DDVISTGGTM KAVIKALEKA GAVIKDIVVV IERGDGKKSI EELGYDVQTL IKIDVDENGV
     KILGCIDEEC Q
//

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