ID   HPRT_METRM              Reviewed;         188 AA.
AC   D3DYU7;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 52.
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=mru_0165;
OS   Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS   OCM 146 / M1) (Methanobacterium ruminantium).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=634498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1;
RX   PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA   Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA   Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA   Janssen P.H., Dey D., Attwood G.T.;
RT   "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT   reveals new possibilities for controlling ruminant methane emissions.";
RL   PLoS ONE 5:E8926-E8926(2010).
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; CP001719; ADC46017.1; -; Genomic_DNA.
DR   RefSeq; WP_012954973.1; NC_013790.1.
DR   AlphaFoldDB; D3DYU7; -.
DR   SMR; D3DYU7; -.
DR   STRING; 634498.mru_0165; -.
DR   EnsemblBacteria; ADC46017; ADC46017; mru_0165.
DR   GeneID; 8769784; -.
DR   KEGG; mru:mru_0165; -.
DR   PATRIC; fig|634498.28.peg.170; -.
DR   eggNOG; arCOG00030; Archaea.
DR   HOGENOM; CLU_126376_0_0_2; -.
DR   OMA; FIHPISD; -.
DR   OrthoDB; 88302at2157; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000008680; 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..188
FT                   /note="Hypoxanthine/guanine phosphoribosyltransferase"
FT                   /id="PRO_0000415465"
SQ   SEQUENCE   188 AA;  20346 MW;  CA07E7E9D84AA1C9 CRC64;
     MLENLVESLR NAPVVKKGDY DYFVHGISDG IPALNPCVLK EISEVLAERI DLDKVDKIVG
     VEAMGIHIAT ALSLETGLPL LVIRKREYGL EGEHEILKHT GYATSKLYIN DLNEGDNIVL
     VDDVVSTGGT LSVVINELKA IGVNILDTFV VVEKGEGKKI VEDKTGENIV TLVKLDVVDG
     KVVADSLI