[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0014-5793(96)00902-7; PubMed=8814303 [NCBI, ExPASy, EBI, Israel, Japan] Lee M.H., Zhang Z.H., MacKinnon C.H., Baldwin J.E., Crouch N.P.; "The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity."; FEBS Lett. 393:269-272(1996).
[2]	NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT THR-2, AND SUBCELLULAR LOCATION. DOI=10.1016/S1065-6995(03)00117-3; PubMed=12867153 [NCBI, ExPASy, EBI, Israel, Japan] Neve S., Aarenstrup L., Tornehave D., Rahbek-Nielsen H., Corydon T.J., Roepstorff P., Kristiansen K.; "Tissue distribution, intracellular localization and proteolytic processing of rat 4-hydroxyphenylpyruvate dioxygenase."; Cell Biol. Int. 27:611-624(2003).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 4-393. PubMed=2445820 [NCBI, ExPASy, EBI, Israel, Japan] Gershwin M.E., Coppel R.L., Bearer E., Peterson M.G., Sturgess A., McKay I.R.; "Molecular cloning of the liver-specific rat F antigen."; J. Immunol. 139:3828-3833(1987).
[5]	X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH INHIBITOR DAS869, BIOPHYSICOCHEMICAL PROPERTIES, METAL-BINDING SITES, AND SUBUNIT. DOI=10.1021/bi049323o; PubMed=15301540 [NCBI, ExPASy, EBI, Israel, Japan] Yang C., Pflugrath J.W., Camper D.L., Foster M.L., Pernich D.J., Walsh T.A.; "Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases."; Biochemistry 43:10414-10423(2004).

Comments

CATALYTIC ACTIVITY: 4-hydroxyphenylpyruvate + O₂ = homogentisate + CO₂.
COFACTOR: Binds 1 iron ion per subunit.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=13 µM for HPPA;
PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein.
SIMILARITY: Belongs to the 4HPPD family.
SEQUENCE CAUTION:
- Sequence=AAA40740.1; Type=Frameshift; Positions=381;

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

AF082834; AAC32387.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081819; AAH81819.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18405; AAA40740.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S32820; S32820.
S74178; S74178.

RefSeq

NP_058929.1; -.

UniGene

Rn.3664

3D structure databases

PDB

1SQI; X-ray; 2.15 A; A/B=1-393.

[ExPASy / RCSB / EBI]

PDBsum

1SQI; -.

ModBase

P32755.

Protein-protein interaction databases

IntAct

P32755; -.

Organism-specific databases

RGD

61974; Hpd.

GeneLynx

Hpd; Rattus norvegicus.

Gene expression databases

ArrayExpress

P32755; -.

GermOnline

ENSRNOG00000001338; Rattus norvegicus.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (inferred from direct assay from MGI).
GO:0005794;	Cellular component: Golgi apparatus (inferred from direct assay from MGI).
GO:0003868;	Molecular function: 4-hydroxyphenylpyruvate dioxygenase activity (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR004360; Glyas_bleo-R_dOase.
IPR005956; HPP_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

P32755.

Genome annotation databases

Ensembl

ENSRNOG00000001338; Rattus norvegicus. [Contig view]

GeneID

29531; -.

KEGG

rno:29531; -.

NMPDR

fig|10116.3.peg.8568; -.

Other

ProtoNet

P32755.

UniRef

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

Keywords

3D-structure; Acetylation; Cytoplasm; Dioxygenase; Endoplasmic reticulum; Golgi apparatus; Iron; Membrane; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Phosphoprotein; Tyrosine catabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 393`	`392`	`4-hydroxyphenylpyruvate dioxygenase.`	`PRO_0000088391`
`METAL`	`183 183`		`Iron.`
`METAL`	`266 266`		`Iron.`
`METAL`	`349 349`		`Iron.`
`MOD_RES`	`2 2`		`N-acetylthreonine.`
`MOD_RES`	`250 250`		`Phosphoserine (By similarity).`
`CONFLICT`	`5 6`		`SN -> WD (in Ref. 4; AAA40740).`
`STRAND`	`15 25`	`11`
`HELIX`	`29 40`	`12`
`STRAND`	`43 49`	`7`
`HELIX`	`50 52`	`3`
`STRAND`	`56 64`	`9`
`STRAND`	`67 76`	`10`
`HELIX`	`80 89`	`10`
`STRAND`	`91 101`	`11`
`HELIX`	`103 113`	`11`
`STRAND`	`117 126`	`10`
`STRAND`	`129 137`	`9`
`STRAND`	`143 151`	`9`
`STRAND`	`154 157`	`4`
`HELIX`	`170 172`	`3`
`STRAND`	`178 187`	`10`
`HELIX`	`193 204`	`12`
`STRAND`	`207 209`	`3`
`STRAND`	`225 230`	`6`
`STRAND`	`237 242`	`6`
`HELIX`	`251 259`	`9`
`STRAND`	`261 272`	`12`
`HELIX`	`274 284`	`11`
`HELIX`	`293 304`	`12`
`HELIX`	`314 320`	`7`
`STRAND`	`323 325`	`3`
`STRAND`	`331 337`	`7`
`STRAND`	`340 344`	`5`
`STRAND`	`347 355`	`9`
`HELIX`	`361 365`	`5`

Sequence information

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

Molecular weight: 45112 Da [This is the MW of the unprocessed precursor]

CRC64: E8D1B7B9FC4C0EC3 [This is a checksum on the sequence]

        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

P32755 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