ID HPRT_METV3 Reviewed; 187 AA. AC D7DQT8; DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot. DT 10-AUG-2010, sequence version 1. DT 27-MAR-2024, entry version 61. 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}; GN OrderedLocusNames=Mvol_1560; OS Methanococcus voltae (strain ATCC BAA-1334 / A3). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=456320; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1334 / A3; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Whitman W.B., Woyke T.; RT "Complete sequence of Methanococcus voltae A3."; RL Submitted (MAY-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}. 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; CP002057; ADI37215.1; -; Genomic_DNA. DR AlphaFoldDB; D7DQT8; -. DR SMR; D7DQT8; -. DR STRING; 456320.Mvol_1560; -. DR KEGG; mvo:Mvol_1560; -. DR eggNOG; arCOG00030; Archaea. DR HOGENOM; CLU_126376_0_0_2; -. DR InParanoid; D7DQT8; -. DR OrthoDB; 8323at2157; -. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000007722; 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. PE 3: Inferred from homology; KW Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome; KW Transferase. FT CHAIN 1..187 FT /note="Hypoxanthine/guanine phosphoribosyltransferase" FT /id="PRO_0000415473" SQ SEQUENCE 187 AA; 20529 MW; AC96BF37D4D189D4 CRC64; MKKVLDETLE SSPIIKRGEY NYFIHPIADG VPLFTSDLLR DVATRTIQRI DTNIDKIVTA EAMGIPIATA ISMSTDIPYV VMRKRQYFLE GEVPVHQETG YSKGELYLNG VEKGDRVTIV DDVLSTGGTL IAVIKALEKA GAEIVDIVCV IERGDGKSKV KEITGYDVQT LVKIDVTENG VVILESN //