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O33799 (HPRT_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Hypoxanthine phosphoribosyltransferase

Short name=HPRT
EC=2.4.2.8
Gene names
Name:hpt
Ordered Locus Names:STM0170
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts preferentially on hypoxanthine; has very low activity towards guanine. Inactive towards xanthine By similarity.

Catalytic activity

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.

Cofactor

Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein By similarity.

Pathway

Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178Hypoxanthine phosphoribosyltransferase
PRO_0000139635

Regions

Nucleotide binding99 – 10810IMP By similarity
Nucleotide binding158 – 1592IMP By similarity

Sites

Active site1031Proton acceptor By similarity
Metal binding1591Magnesium By similarity
Binding site1311IMP By similarity
Binding site1531IMP; via carbonyl oxygen By similarity

Secondary structure

........................... 178
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O33799 [UniParc].

Last modified August 1, 1998. Version 2.
Checksum: 5A52E93CAB331357

FASTA17820,068
        10         20         30         40         50         60 
MKHTVEVMIP EAEIKARIAE LGRQITERYK DSGSEMVLVG LLRGSFMFMA DLCREVQVPH 

        70         80         90        100        110        120 
EVDFMTASSY GSGMSTTRDV KILKDLDEDI RGKDVLIVED IIDSGNTLSK VREILGLREP 

       130        140        150        160        170 
KSLAICTLLD KPSRREVDVP VEFVGFSIPD EFVVGYGIDY AQRYRHLPYV GKVVLLDE 

« Hide

References

« Hide 'large scale' references
[1]"A single amino acid substitution in the human and a bacterial hypoxanthine phosphoribosyltransferase modulates specificity for the binding of guanine."
Lee C.C., Craig S.P. III, Eakin A.E.
Biochemistry 37:3491-3498(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2 / GP660.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Crystal structure of the HPRT from Salmonella typhimurium at 2.3 A resolution."
Lee C.C., Focia P.J., Spraggon G., Eakin A.E.
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF008931 Genomic DNA. Translation: AAC46255.1.
AE006468 Genomic DNA. Translation: AAL19134.1.
RefSeqNP_459175.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J7JX-ray2.30A/B1-178[»]
ProteinModelPortalO33799.
SMRO33799. Positions 1-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM0170.

Proteomic databases

PaxDbO33799.
PRIDEO33799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19134; AAL19134; STM0170.
GeneID1251688.
KEGGstm:STM0170.
PATRIC32378621. VBISalEnt20916_0180.

Phylogenomic databases

eggNOGCOG0634.
HOGENOMHOG000236520.
KOK00760.
OMAVDFMTVS.
OrthoDBEOG693GNP.
PhylomeDBO33799.

Enzyme and pathway databases

BioCycSENT99287:GCTI-169-MONOMER.
UniPathwayUPA00591; UER00648.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
InterProIPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
TIGRFAMsTIGR01203. HGPRTase. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO33799.

Entry information

Entry nameHPRT_SALTY
AccessionPrimary (citable) accession number: O33799
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways