ID HPRT_SALTY Reviewed; 178 AA. AC O33799; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 2. DT 27-MAR-2024, entry version 145. DE RecName: Full=Hypoxanthine phosphoribosyltransferase; DE Short=HPRT; DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P0A9M2}; GN Name=hpt; OrderedLocusNames=STM0170; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2 / GP660; RX PubMed=9521670; DOI=10.1021/bi9720179; RA Lee C.C., Craig S.P. III, Eakin A.E.; RT "A single amino acid substitution in the human and a bacterial hypoxanthine RT phosphoribosyltransferase modulates specificity for the binding of RT guanine."; RL Biochemistry 37:3491-3498(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND RP COFACTOR. RA Lee C.C., Focia P.J., Spraggon G., Eakin A.E.; RT "Crystal structure of the HPRT from Salmonella typhimurium at 2.3 A RT resolution."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Purine salvage pathway enzyme which 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 hypoxanthine to yield IMP CC (inosine 5'-monophosphate). To a lesser extent, can also act on guanine CC leading to GMP, but shows a highly less efficient activity with CC xanthine. {ECO:0000250|UniProtKB:P0A9M2}. 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:P0A9M2}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975; CC Evidence={ECO:0000250|UniProtKB:P0A9M2}; 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:P0A9M2}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426; CC Evidence={ECO:0000250|UniProtKB:P0A9M2}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|Ref.3}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP CC from hypoxanthine: step 1/1. {ECO:0000250|UniProtKB:P0A9M2}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9M2}. 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; AF008931; AAC46255.1; -; Genomic_DNA. DR EMBL; AE006468; AAL19134.1; -; Genomic_DNA. DR RefSeq; NP_459175.1; NC_003197.2. DR RefSeq; WP_000683342.1; NC_003197.2. DR PDB; 1J7J; X-ray; 2.30 A; A/B=1-178. DR PDBsum; 1J7J; -. DR AlphaFoldDB; O33799; -. DR SMR; O33799; -. DR STRING; 99287.STM0170; -. DR PaxDb; 99287-STM0170; -. DR GeneID; 1251688; -. DR KEGG; stm:STM0170; -. DR PATRIC; fig|99287.12.peg.180; -. DR HOGENOM; CLU_073615_0_0_6; -. DR OMA; MQWRVAP; -. DR PhylomeDB; O33799; -. DR BioCyc; SENT99287:STM0170-MONOMER; -. DR UniPathway; UPA00591; UER00648. DR EvolutionaryTrace; O33799; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0032263; P:GMP salvage; IBA:GO_Central. DR GO; GO:0006178; P:guanine salvage; IBA:GO_Central. DR GO; GO:0046100; P:hypoxanthine metabolic process; IBA:GO_Central. DR GO; GO:0032264; P:IMP salvage; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding; KW Nucleotide-binding; Purine salvage; Reference proteome; Transferase. FT CHAIN 1..178 FT /note="Hypoxanthine phosphoribosyltransferase" FT /id="PRO_0000139635" FT ACT_SITE 103 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 43 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 44 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 99 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 99 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 99 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:1J7J" FT BINDING 100 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:1J7J" FT BINDING 103..108 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 103..108 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 131 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 131 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 159 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 165 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:1J7J" FT HELIX 11..30 FT /evidence="ECO:0007829|PDB:1J7J" FT STRAND 36..41 FT /evidence="ECO:0007829|PDB:1J7J" FT TURN 42..45 FT /evidence="ECO:0007829|PDB:1J7J" FT HELIX 46..53 FT /evidence="ECO:0007829|PDB:1J7J" FT STRAND 61..66 FT /evidence="ECO:0007829|PDB:1J7J" FT STRAND 93..104 FT /evidence="ECO:0007829|PDB:1J7J" FT HELIX 106..116 FT /evidence="ECO:0007829|PDB:1J7J" FT STRAND 121..130 FT /evidence="ECO:0007829|PDB:1J7J" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:1J7J" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:1J7J" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:1J7J" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:1J7J" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:1J7J" SQ SEQUENCE 178 AA; 20068 MW; 5A52E93CAB331357 CRC64; MKHTVEVMIP EAEIKARIAE LGRQITERYK DSGSEMVLVG LLRGSFMFMA DLCREVQVPH EVDFMTASSY GSGMSTTRDV KILKDLDEDI RGKDVLIVED IIDSGNTLSK VREILGLREP KSLAICTLLD KPSRREVDVP VEFVGFSIPD EFVVGYGIDY AQRYRHLPYV GKVVLLDE //