ID   HPRT_METSG              Reviewed;         189 AA.
AC   F4BT36;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, 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=MCON_2988;
OS   Methanothrix soehngenii (strain ATCC 5969 / DSM 3671 / JCM 10134 / NBRC
OS   103675 / OCM 69 / GP-6) (Methanosaeta concilii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=990316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 5969 / DSM 3671 / JCM 10134 / NBRC 103675 / OCM 69 / GP-6;
RX   PubMed=21571998; DOI=10.1128/jb.05031-11;
RA   Barber R.D., Zhang L., Harnack M., Olson M.V., Kaul R., Ingram-Smith C.,
RA   Smith K.S.;
RT   "Complete genome sequence of Methanosaeta concilii, a specialist in
RT   aceticlastic methanogenesis.";
RL   J. Bacteriol. 193:3668-3669(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; CP002565; AEB69325.1; -; Genomic_DNA.
DR   RefSeq; WP_013720346.1; NC_015416.1.
DR   AlphaFoldDB; F4BT36; -.
DR   SMR; F4BT36; -.
DR   STRING; 990316.MCON_2988; -.
DR   EnsemblBacteria; AEB69325; AEB69325; MCON_2988.
DR   GeneID; 10462281; -.
DR   KEGG; mcj:MCON_2988; -.
DR   HOGENOM; CLU_126376_0_0_2; -.
DR   OMA; FIHPISD; -.
DR   OrthoDB; 88302at2157; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000007807; 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..189
FT                   /note="Hypoxanthine/guanine phosphoribosyltransferase"
FT                   /id="PRO_0000415477"
SQ   SEQUENCE   189 AA;  20817 MW;  9521B804266A6D86 CRC64;
     MLERLKKSLL EAPVFKRGEY DYFIHPITDG VPEIRPDLIR EVTANIVRIA NLDVDKIVTV
     EAMGIPIGIV LSILCDIPLV IIRKRKYGLP NEVEISQVTG YSRSQLYLNG INRGDRVIVV
     DDVISTGGTL QATLDSMELA GAEVMDTVIV VERGNGAELL RSKGYNLKTM VRVKVEGGRV
     SEVEPGISK