ID   HPRT_METTM              Reviewed;         193 AA.
AC   O33174; D9PYH7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Hypoxanthine/guanine phosphoribosyltransferase;
DE            Short=HGPRTase;
DE            EC=2.4.2.8 {ECO:0000269|PubMed:10074097};
DE   AltName: Full=Hypoxanthine (guanine) phosphoribosyltransferase;
GN   Name=hpt {ECO:0000303|PubMed:10074097}; OrderedLocusNames=MTBMA_c17060;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION AS AN
RP   HGPRTASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=10074097; DOI=10.1128/jb.181.6.1958-1962.1999;
RA   Sauer J., Nygaard P.;
RT   "Expression of the Methanobacterium thermoautotrophicum hpt gene, encoding
RT   hypoxanthine (Guanine) phosphoribosyltransferase, in Escherichia coli.";
RL   J. Bacteriol. 181:1958-1962(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC       IMP that is energically less costly than de novo synthesis. Prefers
CC       hypoxanthine, has 66% activity with guanine while activity with
CC       adenine, xanthine, uracil, orotate, or cytosine is negligible.
CC       {ECO:0000269|PubMed:10074097}.
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:0000269|PubMed:10074097};
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:0000269|PubMed:10074097};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.6-8.2. {ECO:0000269|PubMed:10074097};
CC       Temperature dependence:
CC         Optimum temperature is 70-80 degrees Celsius.
CC         {ECO:0000269|PubMed:10074097};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1. {ECO:0000269|PubMed:10074097}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. Archaeal HPRT subfamily. {ECO:0000305}.
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DR   EMBL; AF007759; AAB62272.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL59275.1; -; Genomic_DNA.
DR   RefSeq; WP_013296485.1; NC_014408.1.
DR   AlphaFoldDB; O33174; -.
DR   SMR; O33174; -.
DR   STRING; 79929.MTBMA_c17060; -.
DR   EnsemblBacteria; ADL59275; ADL59275; MTBMA_c17060.
DR   GeneID; 9705417; -.
DR   KEGG; mmg:MTBMA_c17060; -.
DR   PATRIC; fig|79929.8.peg.1646; -.
DR   HOGENOM; CLU_126376_0_0_2; -.
DR   OMA; FIHPISD; -.
DR   OrthoDB; 88302at2157; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000000345; 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; IDA:UniProtKB.
DR   GO; GO:0043103; P:hypoxanthine salvage; TAS:UniProtKB.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycosyltransferase; Purine salvage;
KW   Transferase.
FT   CHAIN           1..193
FT                   /note="Hypoxanthine/guanine phosphoribosyltransferase"
FT                   /id="PRO_0000149500"
SQ   SEQUENCE   193 AA;  21219 MW;  D2377AC07A276322 CRC64;
     MLDKLKESLR NSPVIKKGEY DYFVNPVTDG IPLTEPELLE EIADEIVRRF NPDPASVDKI
     VCIEAMGIHH ATVLSLKTRI PFVVVRKRRY GLPGEVAVHQ MTGYSEGELY INGVDGDDRV
     MVIDDVVSTG GTLLAVLEAL REMEVEVVDV VTVIDKGEGS RVVKERTGFT VRSLVKADVV
     DGRVTVEDIP DGG