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P0A9M2 (HPRT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hypoxanthine phosphoribosyltransferase

Short name=HPRT
EC=2.4.2.8
Gene names
Name:hpt
Ordered Locus Names:b0125, JW5009
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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. Ref.4

Catalytic activity

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.4

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. Ref.4

Pathway

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

Subunit structure

Homotetramer. Ref.4

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_0000139632

Regions

Nucleotide binding99 – 10810IMP
Nucleotide binding158 – 1592IMP

Sites

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9M2 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: E1A75EB68231DC32

FASTA17820,115
        10         20         30         40         50         60 
MKHTVEVMIP EAEIKARIAE LGRQITERYK DSGSDMVLVG LLRGSFMFMA DLCREVQVSH 

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

       130        140        150        160        170 
KSLAICTLLD KPSRREVNVP VEFIGFSIPD EFVVGYGIDY AQRYRHLPYI GKVILLDE 

« Hide

References

« Hide 'large scale' references
[1]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase."
Guddat L.W., Vos S., Martin J.L., Keough D.T., de Jersey J.
Protein Sci. 11:1626-1638(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEXES WITH IMP; GMP AND MAGNESIUM, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC73236.2.
AP009048 Genomic DNA. Translation: BAB96700.2.
RefSeqNP_414667.4. NC_000913.3.
YP_488428.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G9SX-ray2.80A/B1-178[»]
1G9TX-ray2.80A/B1-178[»]
1GRVX-ray2.90A/B1-178[»]
ProteinModelPortalP0A9M2.
SMRP0A9M2. Positions 1-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47994N.
IntActP0A9M2. 5 interactions.
STRING511145.b0125.

2D gel databases

SWISS-2DPAGEP0A9M2.

Proteomic databases

PaxDbP0A9M2.
PRIDEP0A9M2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73236; AAC73236; b0125.
BAB96700; BAB96700; BAB96700.
GeneID12932685.
946624.
KEGGecj:Y75_p0122.
eco:b0125.
PATRIC32115353. VBIEscCol129921_0128.

Organism-specific databases

EchoBASEEB4143.
EcoGeneEG20098. hpt.

Phylogenomic databases

eggNOGCOG0634.
HOGENOMHOG000236520.
KOK00760.
OMAVDFMTVS.
OrthoDBEOG693GNP.
PhylomeDBP0A9M2.

Enzyme and pathway databases

BioCycEcoCyc:HYPOXANPRIBOSYLTRAN-MONOMER.
ECOL316407:JW5009-MONOMER.
MetaCyc:HYPOXANPRIBOSYLTRAN-MONOMER.
UniPathwayUPA00591; UER00648.

Gene expression databases

GenevestigatorP0A9M2.

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

EvolutionaryTraceP0A9M2.
PROP0A9M2.

Entry information

Entry nameHPRT_ECOLI
AccessionPrimary (citable) accession number: P0A9M2
Secondary accession number(s): P36766
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: June 11, 2014
This is version 79 of the entry and version 1 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene