ID HGPRT_LACLA Reviewed; 183 AA. AC Q02522; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 27-MAR-2024, entry version 134. 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=LL0020; ORFNames=L25115; OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=272623; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CHCC285; RX PubMed=1465108; DOI=10.1007/bf00279381; RA Nilsson D., Lauridsen A.A.; RT "Isolation of purine auxotrophic mutants of Lactococcus lactis and RT characterization of the gene hpt encoding hypoxanthine guanine RT phosphoribosyltransferase."; RL Mol. Gen. Genet. 235:359-364(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL1403; RX PubMed=11337471; DOI=10.1101/gr.gr-1697r; RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "The complete genome sequence of the lactic acid bacterium Lactococcus RT lactis ssp. lactis IL1403."; RL Genome Res. 11:731-753(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. 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; X67015; CAA47404.1; -; Genomic_DNA. DR EMBL; X69123; CAA48876.1; -; Genomic_DNA. DR EMBL; AE005176; AAK04118.1; -; Genomic_DNA. DR PIR; D86627; D86627. DR PIR; S30100; S30100. DR RefSeq; NP_266176.1; NC_002662.1. DR RefSeq; WP_010905038.1; NC_002662.1. DR AlphaFoldDB; Q02522; -. DR SMR; Q02522; -. DR PaxDb; 272623-L25115; -. DR EnsemblBacteria; AAK04118; AAK04118; L25115. DR GeneID; 69712096; -. DR KEGG; lla:L25115; -. DR PATRIC; fig|272623.7.peg.22; -. DR eggNOG; COG0634; Bacteria. DR HOGENOM; CLU_073615_0_1_9; -. DR OrthoDB; 9802824at2; -. DR UniPathway; UPA00591; UER00648. DR UniPathway; UPA00909; UER00887. DR Proteomes; UP000002196; 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..183 FT /note="Hypoxanthine-guanine phosphoribosyltransferase" FT /id="PRO_0000139604" FT ACT_SITE 107 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 47 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 48 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 104 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 134 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 155..156 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 162 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 168 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" SQ SEQUENCE 183 AA; 20648 MW; A9D903FC9E6EBDB7 CRC64; MLEKNLDKAI EKVLVSEEEI IEKSKELGEI LTKEYEGKNP LVLGILRGSV PFLAELIKHI DCHLETDFMT VSSYHGGTKS SGEVKLILDV DTAVKGRDIL IVEDIIDTGR TLKYLKELLE HRGANVKIVT LLDKPEGRIV EIKPDYSGFT IPNEFVVGFG LDYEENYRNL PYVGVLKPEV YNK //