ID   HPRT_METMP              Reviewed;         185 AA.
AC   Q6M0X3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Hypoxanthine/guanine phosphoribosyltransferase;
DE            Short=HGPRTase;
DE            EC=2.4.2.8;
GN   Name=hpt; OrderedLocusNames=MMP0145;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   BIOTECHNOLOGY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=S2 / LL;
RX   PubMed=15659675; DOI=10.1128/jb.187.3.972-979.2005;
RA   Moore B.C., Leigh J.A.;
RT   "Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for
RT   alanine dehydrogenase, alanine racemase, and alanine permease.";
RL   J. Bacteriol. 187:972-979(2005).
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.
CC   -!- DISRUPTION PHENOTYPE: Increased resistance to the base analog 8-
CC       azahypoxanthine. {ECO:0000269|PubMed:15659675}.
CC   -!- BIOTECHNOLOGY: Can be used as a counterselectable marker when
CC       transforming this organism. {ECO:0000269|PubMed:15659675}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. Archaeal HPRT subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX950229; CAF29701.1; -; Genomic_DNA.
DR   RefSeq; WP_011170089.1; NC_005791.1.
DR   AlphaFoldDB; Q6M0X3; -.
DR   SMR; Q6M0X3; -.
DR   STRING; 267377.MMP0145; -.
DR   EnsemblBacteria; CAF29701; CAF29701; MMP0145.
DR   GeneID; 2762740; -.
DR   KEGG; mmp:MMP0145; -.
DR   PATRIC; fig|267377.15.peg.148; -.
DR   eggNOG; arCOG00030; Archaea.
DR   HOGENOM; CLU_126376_0_0_2; -.
DR   OrthoDB; 8323at2157; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000000590; 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   NCBIfam; NF040646; HPT_Archaea; 1.
DR   PANTHER; PTHR43864; HYPOXANTHINE/GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43864:SF1; HYPOXANTHINE_GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 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..185
FT                   /note="Hypoxanthine/guanine phosphoribosyltransferase"
FT                   /id="PRO_0000149498"
SQ   SEQUENCE   185 AA;  20402 MW;  4E99371CB6FE0EC2 CRC64;
     MSKLLEESLK TCPIVKRGEY HYFIHPISDG VPLVEPELLR DVSTRVIKMI DTDVDKIVTA
     EAMGIPIVTA VSIATDIPYV IMRKREYLLE GEIPVHQETG YSKGELYLNG INKGDKVIIL
     DDVISTGGTL VAIINALKRA GADIKDVLCI IDRGNGQNIV EEKTGYKVKT IVKIEVVDGK
     VNILE
//