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 25-MAY-2022, entry version 50.
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}.
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DR EMBL; AP011532; BAI60472.1; -; Genomic_DNA.
DR AlphaFoldDB; D1YVK0; -.
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 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;
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