(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 126.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase;
DE            Short=HPRT;
DE            EC=2.4.2.8;
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.
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: Acts preferentially on hypoxanthine; has very low activity
CC       towards guanine. Inactive towards xanthine (By similarity).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. The magnesium ions are
CC       essentially bound to the substrate and have few direct interactions
CC       with the protein. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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   SMR; O33799; -.
DR   PaxDb; O33799; -.
DR   PRIDE; O33799; -.
DR   EnsemblBacteria; AAL19134; AAL19134; STM0170.
DR   GeneID; 1251688; -.
DR   KEGG; stm:STM0170; -.
DR   PATRIC; fig|99287.12.peg.180; -.
DR   eggNOG; ENOG4108UGV; Bacteria.
DR   eggNOG; COG0634; LUCA.
DR   HOGENOM; HOG000236520; -.
DR   KO; K00760; -.
DR   OMA; TMDWMAV; -.
DR   PhylomeDB; O33799; -.
DR   BioCyc; SENT99287:STM0170-MONOMER; -.
DR   UniPathway; UPA00591; UER00648.
DR   EvolutionaryTrace; O33799; -.
DR   Proteomes; UP000001014; 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; 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:0006168; P:adenine salvage; IBA:GO_Central.
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; IBA:GO_Central.
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;
DR   PRODOM; O33799.
DR   SWISS-2DPAGE; O33799.
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   NP_BIND         99..108
FT                   /note="IMP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         158..159
FT                   /note="IMP"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        103
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   METAL           159
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /note="IMP"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /note="IMP; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   STRAND          4..9
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   HELIX           11..30
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   STRAND          36..41
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   TURN            42..45
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   HELIX           46..53
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   STRAND          61..66
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   STRAND          93..104
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   HELIX           106..116
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   STRAND          121..130
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   HELIX           132..134
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   STRAND          142..147
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   STRAND          153..155
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   STRAND          160..162
FT                   /evidence="ECO:0000244|PDB:1J7J"
FT   STRAND          168..174
FT                   /evidence="ECO:0000244|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
//

If you have problems or comments...

PBIL Back to PBIL home page