ID   HPRT_METAC              Reviewed;         189 AA.
AC   Q8TSS8;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Hypoxanthine/guanine phosphoribosyltransferase;
DE            Short=HGPRTase;
DE            EC=2.4.2.8;
GN   Name=hpt; OrderedLocusNames=MA_0717;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   BIOTECHNOLOGY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=15006762; DOI=10.1128/aem.70.3.1425-1433.2004;
RA   Pritchett M.A., Zhang J.K., Metcalf W.W.;
RT   "Development of a markerless genetic exchange method for Methanosarcina
RT   acetivorans C2A and its use in construction of new genetic tools for
RT   methanogenic archaea.";
RL   Appl. Environ. Microbiol. 70:1425-1433(2004).
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC       IMP that is energically less costly than de novo synthesis.
CC       {ECO:0000250}.
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   -!- 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   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells have increased resistant to purine analogs
CC       8-aza-2,6-diaminopurine (8-ADP) and 2-methylpurine (2MP). No change in
CC       growth rate in HS (minimal) broth. {ECO:0000269|PubMed:15006762}.
CC   -!- BIOTECHNOLOGY: Used for negative selection when transforming this
CC       organism. {ECO:0000269|PubMed:15006762}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. Archaeal HPRT subfamily. {ECO:0000305}.
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DR   EMBL; AE010299; AAM04157.1; -; Genomic_DNA.
DR   RefSeq; WP_011020762.1; NC_003552.1.
DR   AlphaFoldDB; Q8TSS8; -.
DR   SMR; Q8TSS8; -.
DR   STRING; 188937.MA_0717; -.
DR   EnsemblBacteria; AAM04157; AAM04157; MA_0717.
DR   GeneID; 1472609; -.
DR   KEGG; mac:MA_0717; -.
DR   HOGENOM; CLU_126376_0_0_2; -.
DR   InParanoid; Q8TSS8; -.
DR   OMA; FIHPISD; -.
DR   OrthoDB; 88302at2157; -.
DR   PhylomeDB; Q8TSS8; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000002487; 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   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN           1..189
FT                   /note="Hypoxanthine/guanine phosphoribosyltransferase"
FT                   /id="PRO_0000415480"
SQ   SEQUENCE   189 AA;  20673 MW;  3378267CF6A6B848 CRC64;
     MLERLKDSLV NSPVIKRGEY NYFIHPISDG VPSIDPRLIE EIANYIIRIA DMDVDTILTI
     EAMGIPVANA LSLKTGIPLT IVRKRPYFLE GEVELSQSTG YSKGVLYING LKKGDRVVIV
     DDVISTGGTL LALVKALQNM GVEITDVISV IGRGAGYFKL RELGVEPKIL VTIDVSEKGV
     EIQDVFGDQ