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P32755 (HPPD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxyphenylpyruvate dioxygenase
EC=1.13.11.27
Alternative name(s):
4-hydroxyphenylpyruvic acid oxidase
Short name=4HPPD
Short name=HPD
Short name=HPPDase
F Alloantigen
Short name=F protein
Gene names
Name:Hpd
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme in the degradation of tyrosine.

Catalytic activity

4-hydroxyphenylpyruvate + O2 = homogentisate + CO2. Ref.1

Cofactor

Binds 1 iron ion per subunit.

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein Ref.2.

Sequence similarities

Belongs to the 4HPPD family.

Biophysicochemical properties

Kinetic parameters:

KM=13 µM for HPPA Ref.5

Sequence caution

The sequence AAA40740.1 differs from that shown. Reason: Frameshift at position 381.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 3933924-hydroxyphenylpyruvate dioxygenase
PRO_0000088391

Sites

Metal binding1831Iron
Metal binding2661Iron
Metal binding3491Iron

Amino acid modifications

Modified residue21N-acetylthreonine Ref.2
Modified residue2501Phosphoserine By similarity

Experimental info

Sequence conflict5 – 62SN → WD in AAA40740. Ref.4

Secondary structure

1 .......................................................... 393
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32755 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E8D1B7B9FC4C0EC3

FASTA39345,112
        10         20         30         40         50         60 
MTTYSNKGPK PERGRFLHFH SVTFWVGNAK QAASFYCNKM GFEPLAYKGL ETGSREVVSH 

        70         80         90        100        110        120 
VIKQGKIVFV LCSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCEHIVQKA RERGAKIVRE 

       130        140        150        160        170        180 
PWVEEDKFGK VKFAVLQTYG DTTHTLVEKI NYTGRFLPGF EAPTYKDTLL PKLPSCNLEI 

       190        200        210        220        230        240 
IDHIVGNQPD QEMESASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVA NYEESIKMPI 

       250        260        270        280        290        300 
NEPAPGRKKS QIQEYVDYNG GAGVQHIALR TEDIITTIRH LRERGMEFLA VPSSYYRLLR 

       310        320        330        340        350        360 
ENLKTSKIQV KENMDVLEEL KILVDYDEKG YLLQIFTKPM QDRPTLFLEV IQRHNHQGFG 

       370        380        390 
AGNFNSLFKA FEEEQALRGN LTDLETNGVR SGM

« Hide

References

« Hide 'large scale' references
[1]"The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity."
Lee M.H., Zhang Z.H., MacKinnon C.H., Baldwin J.E., Crouch N.P.
FEBS Lett. 393:269-272(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
[2]"Tissue distribution, intracellular localization and proteolytic processing of rat 4-hydroxyphenylpyruvate dioxygenase."
Neve S., Aarenstrup L., Tornehave D., Rahbek-Nielsen H., Corydon T.J., Roepstorff P., Kristiansen K.
Cell Biol. Int. 27:611-624(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT THR-2, SUBCELLULAR LOCATION.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"Molecular cloning of the liver-specific rat F antigen."
Gershwin M.E., Coppel R.L., Bearer E., Peterson M.G., Sturgess A., McKay I.R.
J. Immunol. 139:3828-3833(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-393.
[5]"Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases."
Yang C., Pflugrath J.W., Camper D.L., Foster M.L., Pernich D.J., Walsh T.A.
Biochemistry 43:10414-10423(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH INHIBITOR DAS869, BIOPHYSICOCHEMICAL PROPERTIES, METAL-BINDING SITES, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF082834 mRNA. Translation: AAC32387.1.
BC081819 mRNA. Translation: AAH81819.1.
M18405 mRNA. Translation: AAA40740.1. Frameshift.
IPIIPI00211507.
PIRS32820.
S74178.
RefSeqNP_058929.1. NM_017233.1.
UniGeneRn.3664.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SQIX-ray2.15A/B1-393[»]
ProteinModelPortalP32755.
SMRP32755. Positions 8-366.
ModBaseSearch...

Proteomic databases

PaxDbP32755.
PRIDEP32755.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001809; ENSRNOP00000001809; ENSRNOG00000001338.
GeneID29531.
KEGGrno:29531.
UCSCRGD:61974. rat.

Organism-specific databases

CTD3242.
RGD61974. Hpd.

Phylogenomic databases

eggNOGCOG3185.
GeneTreeENSGT00530000063474.
HOGENOMHOG000188687.
HOVERGENHBG005987.
InParanoidP32755.
KOK00457.
OrthoDBEOG4Q58PF.

Enzyme and pathway databases

BRENDA1.13.11.27. 5301.
UniPathwayUPA00139; UER00362.

Gene expression databases

ArrayExpressP32755.
GenevestigatorP32755.
GermOnlineENSRNOG00000001338. Rattus norvegicus.

Family and domain databases

InterProIPR005956. 4OHPhenylPyrv_dOase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]
PANTHERPTHR11959. PTHR11959. 1 hit.
PfamPF00903. Glyoxalase. 2 hits.
[Graphical view]
PIRSFPIRSF009283. HPP_dOase. 1 hit.
TIGRFAMsTIGR01263. 4HPPD. 1 hit.
ProtoNetSearch...

Other

BindingDBP32755.
ChEMBLCHEMBL5863.
EvolutionaryTraceP32755.
NextBio609504.

Entry information

Entry nameHPPD_RAT
AccessionPrimary (citable) accession number: P32755
Secondary accession number(s): O88655
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

Recent format changes (XML)

Overview of recent format changes in the XML format

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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