[1]	PROTEIN SEQUENCE. PubMed=1572351 [NCBI, ExPASy, EBI, Israel, Japan] Rueetschi U., Odelhoeg B., Lindstedt S., Barros-Soederling J., Persson B., Joernvall H.; "Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme."; Eur. J. Biochem. 205:459-466(1992).
[2]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1016/S0969-2126(99)80124-5; PubMed=10467142 [NCBI, ExPASy, EBI, Israel, Japan] Serre L., Sailland A., Sy D., Boudec P., Rolland A., Pebay-Peyroula E., Cohen-Addad C.; "Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway."; Structure 7:977-988(1999).

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: Homotetramer.
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

PIR

S21209; S21209.

3D structure databases

PDB

1CJX; X-ray; 2.40 A; A/B/C/D=1-357.

[ExPASy / RCSB / EBI]

PDBsum

1CJX; -.

ModBase

P80064.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12032; -.

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; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF009283; HPP_dOase; 1.

TIGR01263; 4HPPD; 1.

Other

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

Keywords

3D-structure; Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Tyrosine catabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 357`	`357`	`4-hydroxyphenylpyruvate dioxygenase.`	`PRO_0000088408`
`COMPBIAS`	`167 196`	`30`	`Tyr-rich.`
`METAL`	`161 161`		`Iron.`
`METAL`	`240 240`		`Iron.`
`METAL`	`322 322`		`Iron.`
`STRAND`	`10 19`	`10`
`HELIX`	`27 32`	`6`
`STRAND`	`36 51`	`16`
`STRAND`	`54 59`	`6`
`STRAND`	`62 64`	`3`
`HELIX`	`65 73`	`9`
`STRAND`	`74 85`	`12`
`HELIX`	`87 96`	`10`
`STRAND`	`115 117`	`3`
`HELIX`	`119 121`	`3`
`STRAND`	`123 127`	`5`
`STRAND`	`131 133`	`3`
`HELIX`	`136 140`	`5`
`STRAND`	`141 143`	`3`
`STRAND`	`155 162`	`8`
`HELIX`	`170 182`	`13`
`STRAND`	`185 193`	`9`
`STRAND`	`198 205`	`8`
`STRAND`	`212 218`	`7`
`HELIX`	`225 233`	`9`
`STRAND`	`235 237`	`3`
`STRAND`	`240 246`	`7`
`HELIX`	`248 257`	`10`
`HELIX`	`268 272`	`5`
`HELIX`	`274 277`	`4`
`HELIX`	`285 291`	`7`
`STRAND`	`294 300`	`7`
`STRAND`	`303 312`	`10`
`STRAND`	`319 328`	`10`
`HELIX`	`334 351`	`18`

Sequence information

Length: 357 AA [This is the length of the unprocessed precursor]

Molecular weight: 40061 Da [This is the MW of the unprocessed precursor]

CRC64: 26CF4A80B1484BD0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
ADLYENPMGL MGFEFIELAS PTPNTLEPIF EIMGFTKVAT HRSKDVHLYR QGAINLILNN 

        70         80         90        100        110        120 
EPHSVASYFA AEHGPSVCGM AFRVKDSQKA YKRALELGAQ PIHIETGPME LNLPAIKGIG 

       130        140        150        160        170        180 
GAPLYLIDRF GEGSSIYDID FVFLEGVDRH PVGAGLKIID HLTHNVYRGR MAYWANFYEK 

       190        200        210        220        230        240 
LFNFREIRYF DIKGEYTGLT SKAMTAPDGM IRIPLNEESS KGAGQIEEFL MQFNGEGIQH 

       250        260        270        280        290        300 
VAFLSDDLIK TWDHLKSIGM RFMTAPPDTY YEMLEGRLPN HGEPVGELQA RGILLDGSSE 

       310        320        330        340        350 
SGDKRLLLQI FSETLMGPVF FEFIQRKGDD GFGEGNFKAL FESIERDQVR RGVLSTD

P80064 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