HPRT_METMS
ID HPRT_METMS Reviewed; 190 AA.
AC D5E7U7;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
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=Mmah_1740;
OS Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX NCBI_TaxID=547558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35705 / DSM 5219 / SLP;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Methanohalophilus mahii DSM 5219.";
RL Submitted (MAR-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; CP001994; ADE37235.1; -; Genomic_DNA.
DR RefSeq; WP_013038177.1; NC_014002.1.
DR AlphaFoldDB; D5E7U7; -.
DR SMR; D5E7U7; -.
DR STRING; 547558.Mmah_1740; -.
DR EnsemblBacteria; ADE37235; ADE37235; Mmah_1740.
DR GeneID; 8983922; -.
DR KEGG; mmh:Mmah_1740; -.
DR HOGENOM; CLU_126376_0_0_2; -.
DR OMA; FIHPISD; -.
DR OrthoDB; 88302at2157; -.
DR UniPathway; UPA00591; UER00648.
DR Proteomes; UP000001059; 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..190
FT /note="Hypoxanthine/guanine phosphoribosyltransferase"
FT /id="PRO_0000415476"
SQ SEQUENCE 190 AA; 20772 MW; 7F8020FBFD2AEE2A CRC64;
MLEILKKSLK KAPIVKRGKY PYFIHPITDG VPAIDPKLLD EISDYIIEYS DMDVDRILSI
EAMGIPLATA ISLKTGIPFS IVRKRQYQLP GEIKISQSTG YSKGELYING IEKGNRILLV
DDVISTGGTL RFLVKALEEK GVTISDIIVI VGRGDGVQQL AGEGIRVKTL VDINVSEDGV
SILEDTGETN