4-hydroxyphenylpyruvate dioxygenase - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P32755 (HPPD_RAT)

Last modified June 16, 2009. Version 78. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    4-hydroxyphenylpyruvate dioxygenase
    EC=1.13.11.27
Alternative name(s):
    4-hydroxyphenylpyruvic acid oxidase
      Short name=HPPDase
      Short name=4HPPD
      Short name=HPD
    F Alloantigen
      Short name=F protein

Gene names

Name:

Hpd

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	4-hydroxyphenylpyruvate + O₂ = homogentisate + CO₂.
Cofactor	Binds 1 iron ion per subunit.
Pathway	Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid 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: K_M=13 µM for HPPA
Sequence caution	The sequence AAA40740.1 differs from that shown. Reason: Frameshift at position 381.

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Ontologies

Keywords
Biological process	Phenylalanine catabolism Tyrosine catabolism
Cellular component	Cytoplasm Endoplasmic reticulum Golgi apparatus Membrane
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tyrosine catabolic process Ref.2 Traceable author statement. Source: RGD
Cellular component	Golgi membrane Ref.2 Inferred from direct assay. Source: RGD endoplasmic reticulum membrane Ref.2 Inferred from direct assay. Source: RGD
Molecular function	4-hydroxyphenylpyruvate dioxygenase activity Ref.2 Inferred from direct assay. Source: MGI iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 393

392

4-hydroxyphenylpyruvate dioxygenase

PRO_0000088391

Sites

Metal binding

183

Iron

Metal binding

266

Iron

Metal binding

349

Iron

Amino acid modifications

Modified residue

N-acetylthreonine Ref.2

Modified residue

250

Phosphoserine By similarity

Experimental info

Sequence conflict

5 – 6

SN → WD in AAA40740. Ref.4

Secondary structure

393

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P32755-1 [UniParc].

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

393

45,112

        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

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References

	« Hide 'large scale' referencesShow '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: 8814303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 12867153] [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: 15489334] [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: 2445820] [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: 15301540] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH INHIBITOR DAS869, BIOPHYSICOCHEMICAL PROPERTIES, METAL-BINDING SITES, SUBUNIT.

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Cross-references

Sequence databases

AF082834 mRNA. Translation: AAC32387.1.
BC081819 mRNA. Translation: AAH81819.1.
M18405 mRNA. Translation: AAA40740.1. Frameshift.

IPI

IPI00211507.

PIR

S32820.
S74178.

RefSeq

NP_058929.1.

UniGene

Rn.3664

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SQI	X-ray	2.15	A/B	1-393	[»]

ModBase

Search...

Proteomic databases

PRIDE

P32755.

Genome annotation databases

Ensembl

ENSRNOG00000001338. Rattus norvegicus. [Contig view]

GeneID

29531.

KEGG

rno:29531.

NMPDR

fig|10116.3.peg.8568.

Organism-specific databases

RGD

61974. Hpd.

Phylogenomic databases

HOVERGEN

P32755.

Enzyme and pathway databases

BRENDA

1.13.11.27. 248.

Gene expression databases

ArrayExpress

P32755.

GermOnline

ENSRNOG00000001338. Rattus norvegicus.

Family and domain databases

InterPro

IPR005956. 4OHPhenylPyrv_dOase.
IPR004360. Glyas_bleo-R_dOase.
[Graphical view]

PANTHER

PTHR11959. HPP_dOase. 1 hit.

Pfam

PF00903. Glyoxalase. 2 hits.
[Graphical view]

PIRSF

PIRSF009283. HPP_dOase. 1 hit.

TIGRFAMs

TIGR01263. 4HPPD. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

609504.

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Entry information

Entry name

HPPD_RAT

Accession

Primary (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:	June 16, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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