[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Rumen reticulum; NIH - Mammalian Gene Collection (MGC) project; Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: 4-hydroxyphenylpyruvate + O₂ = homogentisate + CO₂.
COFACTOR: Binds 1 iron ion per subunit (By similarity).
PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid and fumarate from L-phenylalanine: step 3/6 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the 4HPPD family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BT020749; AAX08766.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105225; AAI05226.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001015611.1; -.

UniGene

Bt.19922

3D structure databases

SMR

Q5EA20; 7-365, 8-366.

ModBase

Q5EA20.

Family and domain databases

InterPro

IPR005956; 4OHPhenylPyrv_dOase.
IPR004360; Glyas_bleo-R_dOase.
Graphical view of domain structure.

PANTHER

PTHR11959; HPP_dOase; 1.

Pfam

PF00903; Glyoxalase; 2.
Pfam graphical view of domain structure.

PIRSF

PIRSF009283; HPP_dOase; 1.

TIGRFAMs

TIGR01263; 4HPPD; 1.

BLOCKS

Q5EA20.

Genome annotation databases

Ensembl

ENSBTAG00000004175; Bos taurus. [Contig view]

GeneID

516058; -.

KEGG

bta:516058; -.

Phylogenomic databases

HOVERGEN

Q5EA20; -.

Other

ProtoNet

Q5EA20.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Phosphoprotein; Tyrosine catabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 393`	`392`	`4-hydroxyphenylpyruvate dioxygenase.`	`PRO_0000088387`
`METAL`	`183 183`		`Iron (By similarity).`
`METAL`	`266 266`		`Iron (By similarity).`
`METAL`	`349 349`		`Iron (By similarity).`
`MOD_RES`	`2 2`		`N-acetylthreonine (By similarity).`
`MOD_RES`	`250 250`		`Phosphoserine (By similarity).`

Sequence information

Length: 393 AA [This is the length of the unprocessed precursor]

Molecular weight: 44963 Da [This is the MW of the unprocessed precursor]

CRC64: 03036A1CD0B7BBD1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTYSDKGEK PERGRFLHFH SVTFWVGNAK QAASYYCSKL GFEPLAYKGL ETGSREVVSH 

        70         80         90        100        110        120 
VVKQGQIVFV FSSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDYIVQKA RERGAKIVRE 

       130        140        150        160        170        180 
PWVEQDKLGK VKFAVLQTYG DTTHTLVEKM NYTGRFLPGF EAPPFMDPQL SKLPSCSLEI 

       190        200        210        220        230        240 
IDHIVGNQPD QEMVSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSVVVA NYEESIKMPI 

       250        260        270        280        290        300 
NEPAPGKKKS QIQEYVDYNG GAGVQHIALK TKDIITAIRH LRERGVEFLA VPSTYYKQLR 

       310        320        330        340        350        360 
EKLKMAKIRV KENIDILEEL KILVDYDEKG YLLQIFTKPM QDRPTLFLEV IQRHNHQGFG 

       370        380        390 
AGNFNSLFKA FEEEQDLRGN LTDMEPNGVV SGM

Q5EA20 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools