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 27-MAR-2024, entry version 59.
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 GeneID; 9132101; -.
DR KEGG; mif:Metin_1083; -.
DR eggNOG; arCOG00030; Archaea.
DR HOGENOM; CLU_126376_0_0_2; -.
DR OrthoDB; 8323at2157; -.
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 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 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
//
