ID HPRT_METRM Reviewed; 188 AA. AC D3DYU7; DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 1. DT 27-MAR-2024, entry version 57. 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=mru_0165; OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OS OCM 146 / M1) (Methanobacterium ruminantium). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter. OX NCBI_TaxID=634498; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1; RX PubMed=20126622; DOI=10.1371/journal.pone.0008926; RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J., RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C., RA Janssen P.H., Dey D., Attwood G.T.; RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium RT reveals new possibilities for controlling ruminant methane emissions."; RL PLoS ONE 5:E8926-E8926(2010). 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; CP001719; ADC46017.1; -; Genomic_DNA. DR RefSeq; WP_012954973.1; NC_013790.1. DR AlphaFoldDB; D3DYU7; -. DR SMR; D3DYU7; -. DR STRING; 634498.mru_0165; -. DR GeneID; 8769784; -. DR KEGG; mru:mru_0165; -. DR PATRIC; fig|634498.28.peg.170; -. DR eggNOG; arCOG00030; Archaea. DR HOGENOM; CLU_126376_0_0_2; -. DR OrthoDB; 8323at2157; -. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000008680; 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; Reference proteome; KW Transferase. FT CHAIN 1..188 FT /note="Hypoxanthine/guanine phosphoribosyltransferase" FT /id="PRO_0000415465" SQ SEQUENCE 188 AA; 20346 MW; CA07E7E9D84AA1C9 CRC64; MLENLVESLR NAPVVKKGDY DYFVHGISDG IPALNPCVLK EISEVLAERI DLDKVDKIVG VEAMGIHIAT ALSLETGLPL LVIRKREYGL EGEHEILKHT GYATSKLYIN DLNEGDNIVL VDDVVSTGGT LSVVINELKA IGVNILDTFV VVEKGEGKKI VEDKTGENIV TLVKLDVVDG KVVADSLI //