ID HGPRT_RHOCB Reviewed; 182 AA. AC P37171; D5AU96; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase; DE Short=HGPRT; DE Short=HGPRTase; DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P9WHQ9}; GN Name=hpt; OrderedLocusNames=RCAP_rcc01790; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Rhodobacter. OX NCBI_TaxID=272942; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=1756169; DOI=10.1016/0167-4781(91)90223-9; RA Beckman D.L., Kranz R.G.; RT "A bacterial homolog to HPRT."; RL Biochim. Biophys. Acta 1129:112-114(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=20418398; DOI=10.1128/jb.00366-10; RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., RA Haselkorn R.; RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium RT Rhodobacter capsulatus SB 1003."; RL J. Bacteriol. 192:3545-3546(2010). CC -!- FUNCTION: Purine salvage pathway enzyme that catalyzes the transfer of CC the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1- CC diphosphate (PRPP) to the N9 position of the 6-oxopurines hypoxanthine CC and guanine to form the corresponding ribonucleotides IMP (inosine 5'- CC monophosphate) and GMP (guanosine 5'-monophosphate), with the release CC of PPi. {ECO:0000250|UniProtKB:P9WHQ9}. 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:0000250|UniProtKB:P9WHQ9}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975; CC Evidence={ECO:0000250|UniProtKB:P9WHQ9}; 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:0000250|UniProtKB:P9WHQ9}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426; CC Evidence={ECO:0000250|UniProtKB:P9WHQ9}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P9WHQ9}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP CC from hypoxanthine: step 1/1. {ECO:0000250|UniProtKB:P9WHQ9}. CC -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP CC from guanine: step 1/1. {ECO:0000250|UniProtKB:P9WHQ9}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase CC family. {ECO:0000305}. 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; X60977; CAA43293.1; -; Genomic_DNA. DR EMBL; CP001312; ADE85535.1; -; Genomic_DNA. DR PIR; S19720; S19720. DR RefSeq; WP_013067514.1; NC_014034.1. DR AlphaFoldDB; P37171; -. DR SMR; P37171; -. DR STRING; 272942.RCAP_rcc01790; -. DR GeneID; 31490665; -. DR KEGG; rcp:RCAP_rcc01790; -. DR eggNOG; COG0634; Bacteria. DR HOGENOM; CLU_073615_0_0_5; -. DR OrthoDB; 9802824at2; -. DR UniPathway; UPA00591; UER00648. DR UniPathway; UPA00909; UER00887. DR Proteomes; UP000002361; 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-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0032263; P:GMP salvage; IEA:UniProtKB-UniPathway. 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 InterPro; IPR005904; Hxn_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR NCBIfam; TIGR01203; HGPRTase; 1. DR PANTHER; PTHR43340:SF1; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR43340; 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; Magnesium; Metal-binding; KW Nucleotide-binding; Purine salvage; Reference proteome; Transferase. FT CHAIN 1..182 FT /note="Hypoxanthine-guanine phosphoribosyltransferase" FT /id="PRO_0000139611" FT ACT_SITE 105 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 45 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 46 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 101 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 102 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 133 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 154..155 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 161 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 167 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" SQ SEQUENCE 182 AA; 20323 MW; 890A60FCE67C0E05 CRC64; MSQSGYVIDQ MISAKAIAAR VEALGAEITE AFKDTDRLVV VGLLRGSFVF IADLIREIGV PCEVDFLEAS SYGNETTSTR EVRVLKDLRG IIGGRDVLVV EDIIDTGHTI SKVMEMLRAR APRRIECCAM LDKPSRREVD VKARWTGFEI PDEFVVGYGL DYAQNHRNLP FIGTVRFTDP QK //