ID   HPRT_METIM              Reviewed;         183 AA.
AC   D5VT38;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   03-AUG-2022, entry version 54.
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=Metin_1083;
OS   Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=573063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11812 / JCM 15783 / ME;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanocaldococcus infernus ME.";
RL   Submitted (APR-2010) 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; CP002009; ADG13741.1; -; Genomic_DNA.
DR   RefSeq; WP_013100486.1; NC_014122.1.
DR   AlphaFoldDB; D5VT38; -.
DR   SMR; D5VT38; -.
DR   STRING; 573063.Metin_1083; -.
DR   EnsemblBacteria; ADG13741; ADG13741; Metin_1083.
DR   GeneID; 9132101; -.
DR   KEGG; mif:Metin_1083; -.
DR   eggNOG; arCOG00030; Archaea.
DR   HOGENOM; CLU_126376_0_0_2; -.
DR   OMA; FIHPISD; -.
DR   OrthoDB; 88302at2157; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000002061; 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_0000415467"
SQ   SEQUENCE   183 AA;  20292 MW;  2AA2CCD386688307 CRC64;
     MKLEESLKKC PVIKRGEYNY FVHPITDGIP LVEPSLLREV ACRILKIVDF SEVDKIVTAE
     AMGIHLATTL SLYTDIPFVI IRKRSYGLEG EIPVFQKTGY SKGQLYVNGI KEGDKVVIVD
     DVISTGGTMI AIIEALKRAG AEIKDIVCVI ERGKGREIVE KKTGYKIKTL VKIDVVDGKV
     VIK