HPRT_METVM
ID HPRT_METVM Reviewed; 183 AA.
AC C9RH78;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 58.
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=Metvu_1072;
OS Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
OS (Methanococcus vulcanius).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=579137;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700851 / DSM 12094 / M7;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Lcollab F.I., Brettin T., Detter J.C.,
RA Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinikova G., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus vulcanius M7.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001787; ACX72930.1; -; Genomic_DNA.
DR RefSeq; WP_015733150.1; NC_013407.1.
DR AlphaFoldDB; C9RH78; -.
DR SMR; C9RH78; -.
DR STRING; 579137.Metvu_1072; -.
DR EnsemblBacteria; ACX72930; ACX72930; Metvu_1072.
DR GeneID; 8513411; -.
DR KEGG; mvu:Metvu_1072; -.
DR eggNOG; arCOG00030; Archaea.
DR HOGENOM; CLU_126376_0_0_2; -.
DR OMA; FIHPISD; -.
DR OrthoDB; 88302at2157; -.
DR UniPathway; UPA00591; UER00648.
DR Proteomes; UP000002063; 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; Transferase.
FT CHAIN 1..183
FT /note="Hypoxanthine/guanine phosphoribosyltransferase"
FT /id="PRO_0000415469"
SQ SEQUENCE 183 AA; 20258 MW; 47C57834F83CF115 CRC64;
MLLEETLKSC PIVKRGKYHY FIHPISDGVP LVEPKLLREV ATRIIKIGNF EGVNKIVTAE
AMGIPLVTTL SLYTDIPYVI MRKREYKLPG EVPVFQSTGY SKGQLYLNGI EKGDKVIIID
DVISTGGTMI AIINALERAG AEIKDIICVI ERGDGKKIVE EKTGYKIKTL VKIDVVDGEV
VIL