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P0A9M3 (HPRT_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:c0154
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Sequence caution

The sequence AAN78648.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPurine salvage
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processIMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

purine ribonucleoside salvage

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionguanine phosphoribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

hypoxanthine phosphoribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178Hypoxanthine phosphoribosyltransferase
PRO_0000139633

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

Sequences

Sequence LengthMass (Da)Tools
P0A9M3 [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

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN78648.1. Different initiation.
RefSeqNP_752104.2. NC_004431.1.

3D structure databases

ProteinModelPortalP0A9M3.
SMRP0A9M3. Positions 1-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c0154.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN78648; AAN78648; c0154.
GeneID1040065.
KEGGecc:c0154.
PATRIC18278384. VBIEscCol75197_0147.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000236520.
KOK00760.
OMAINAHYAD.
OrthoDBEOG693GNP.

Enzyme and pathway databases

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...

Entry information

Entry nameHPRT_ECOL6
AccessionPrimary (citable) accession number: P0A9M3
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 64 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

PATHWAY comments

Index of metabolic and biosynthesis pathways