HPRT_SALTY
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 03-AUG-2022, entry version 137.
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; Proteobacteria; 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}.
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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; O33799; -.
DR EnsemblBacteria; AAL19134; AAL19134; STM0170.
DR GeneID; 1251688; -.
DR KEGG; stm:STM0170; -.
DR PATRIC; fig|99287.12.peg.180; -.
DR HOGENOM; CLU_073615_0_0_6; -.
DR OMA; TMDWMAV; -.
DR PhylomeDB; O33799; -.
DR BioCyc; SENT99287:STM0170-MON; -.
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 Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01203; HGPRTase; 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 REGION 43..44
FT /note="Diphosphate"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
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
