ID HPRT_METPW Reviewed; 190 AA. AC F6D512; DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 1. DT 27-MAR-2024, entry version 51. 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=MSWAN_2285; OS Methanobacterium paludis (strain DSM 25820 / JCM 18151 / SWAN1). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanobacterium. OX NCBI_TaxID=868131; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25820 / JCM 18151 / SWAN1; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Chertkov O., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Cadillo-Quiroz H., RA Imachi H., Zinder S., Liu W., Woyke T.; RT "Complete sequence of Methanobacterium sp. SWAN-1."; RL Submitted (MAY-2011) 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; CP002772; AEG19291.1; -; Genomic_DNA. DR RefSeq; WP_013826790.1; NC_015574.1. DR AlphaFoldDB; F6D512; -. DR SMR; F6D512; -. DR STRING; 868131.MSWAN_2285; -. DR GeneID; 10669814; -. DR KEGG; mew:MSWAN_2285; -. DR eggNOG; arCOG00030; Archaea. DR HOGENOM; CLU_126376_0_0_2; -. DR OrthoDB; 8323at2157; -. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000009231; 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..190 FT /note="Hypoxanthine/guanine phosphoribosyltransferase" FT /id="PRO_0000415464" SQ SEQUENCE 190 AA; 20343 MW; 99873CB2BE2460C3 CRC64; MFEKLKKSLI EAPVVKKGDY DYFVHPITDG VPLVVPEILE EVADGVSKFG NMNVDKIVCV EAMGIHIATA LSLKTGIPFV VVRKRSYGLE GEVAVHQMTG YSEGELYING LNSGDRIILV DDVVSTGGTM IAVLKALKAI KVDIVDVMAV IEKGKGKCIV EDATGVTVRS LVKLNVVNGK VVIKGSIDES //