ID   HPRT_METTP              Reviewed;         190 AA.
AC   A0B870;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Mthe_1111;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) 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; CP000477; ABK14894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B870; -.
DR   SMR; A0B870; -.
DR   STRING; 349307.Mthe_1111; -.
DR   EnsemblBacteria; ABK14894; ABK14894; Mthe_1111.
DR   KEGG; mtp:Mthe_1111; -.
DR   HOGENOM; CLU_126376_0_0_2; -.
DR   OMA; FIHPISD; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000000674; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN           1..190
FT                   /note="Hypoxanthine/guanine phosphoribosyltransferase"
FT                   /id="PRO_0000415478"
SQ   SEQUENCE   190 AA;  20888 MW;  F9262748F6837D32 CRC64;
     MLEILKRSLY DAPVFKRGDY NYFIHPITDG VPETRPELIR EVVCHIIRIA DLDVDKIVTV
     EAMGIPIGGA LSLVTDIPLV IIRKKMYGLP GEIEVSQVTG YSKSKIYLNG IKKGDRVIFV
     DDVVSTGGTA IAVMKALEAA GAVIRDAVVV IERGAGAERV RSAGYPLKTM VKVDVDEKRV
     FRVEEVSFRS