ID HGPRT_MYCLE Reviewed; 203 AA. AC O69537; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 2. DT 24-JAN-2024, entry version 116. 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; Synonyms=hprT; OrderedLocusNames=ML0214; OS Mycobacterium leprae (strain TN). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=272631; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN; RX PubMed=11234002; DOI=10.1038/35059006; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). 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 {ECO:0000250}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA18804.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAC29722.1; Type=Erroneous initiation; Evidence={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; AL023093; CAA18804.1; ALT_INIT; Genomic_DNA. DR EMBL; AL583917; CAC29722.1; ALT_INIT; Genomic_DNA. DR PIR; F86935; F86935. DR RefSeq; WP_041323640.1; NC_002677.1. DR AlphaFoldDB; O69537; -. DR SMR; O69537; -. DR STRING; 272631.gene:17574031; -. DR KEGG; mle:ML0214; -. DR Leproma; ML0214; -. DR eggNOG; COG0634; Bacteria. DR HOGENOM; CLU_073615_0_0_11; -. DR UniPathway; UPA00591; UER00648. DR UniPathway; UPA00909; UER00887. DR Proteomes; UP000000806; 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..203 FT /note="Hypoxanthine-guanine phosphoribosyltransferase" FT /id="PRO_0000139608" FT ACT_SITE 126 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 66 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 67 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 122 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 123 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 154 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 175..176 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 182 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 188 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" SQ SEQUENCE 203 AA; 22665 MW; AC9133B56D09EC7A CRC64; MLVAQSFSAI NPGPTAELYL GDIKSVMLTQ EQIQARIAEL GAQIGHDYRD RSPASDQDLL LVTVLKGAVI FVTDLARAIP LPTQFEFMAV SSYGSSMSSS GVVRILKDLD RDIHDRNVLI VEDVVDSGLT LSWLLRNLAT RRPQSLQVCT LLRKPDALRA NVDITYVGFD IPNDFVVGYG LDYDERYRDL PYIGMLDPRV YQQ //