[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2869038 [NCBI, ExPASy, EBI, Israel, Japan] Dahl H.-H.M., Mercer J.F.B.; "Isolation and sequence of a cDNA clone which contains the complete coding region of rat phenylalanine hydroxylase. Structural homology with tyrosine hydroxylase, glucocorticoid regulation, and use of alternate polyadenylation sites."; J. Biol. Chem. 261:4148-4153(1986).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 12-21. TISSUE=Liver; PubMed=7387651 [NCBI, ExPASy, EBI, Israel, Japan] Wretborn M., Humble E., Ragnarsson U., Engstrom L.; "Amino acid sequence at the phosphorylated site of rat liver phenylalanine hydroxylase and phosphorylation of a corresponding synthetic peptide."; Biochem. Biophys. Res. Commun. 93:403-408(1980).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 208-453. DOI=10.1021/bi00319a001; PubMed=6098294 [NCBI, ExPASy, EBI, Israel, Japan] Robson K.J.H., Beattie W., James R.J., Cotton R.C.H., Morgan F.J., Woo S.L.C.; "Sequence comparison of rat liver phenylalanine hydroxylase and its cDNA clones."; Biochemistry 23:5671-5675(1984).
[4]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1038/8247; PubMed=10331871 [NCBI, ExPASy, EBI, Israel, Japan] Kobe B., Jennings I.G., House C.M., Michell B.J., Goodwill K.E., Santarsiero B.D., Stevens R.C., Cotton R.G., Kemp B.E.; "Structural basis of autoregulation of phenylalanine hydroxylase."; Nat. Struct. Biol. 6:442-448(1999).

Comments

CATALYTIC ACTIVITY: L-phenylalanine + tetrahydrobiopterin + O₂ = L-tyrosine + 4a-hydroxytetrahydrobiopterin.
COFACTOR: Fe(2+) ion.
ENZYME REGULATION: N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule.
PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid and fumarate from L-phenylalanine: step 1/6 .
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.
SIMILARITY: Contains 1 ACT domain.

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

M12337; AAA41843.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K02599; AAA41794.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A25321; WHRTF.

UniGene

Rn.1652

3D structure databases

PDB

1PHZ; X-ray; 2.20 A; A=1-429.	[ExPASy / RCSB / EBI]
2PHM; X-ray; 2.60 A; A=1-429.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1PHZ; -.
2PHM; -.

PTM databases

P04176; -.

Organism-specific databases

RGD

3248; Pah.

Gene expression databases

ArrayExpress

P04176; -.

GermOnline

ENSRNOG00000004302; Rattus norvegicus.

Ontologies

GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001273; Aaa_hydroxylase.
IPR002912; ACT_bd.
IPR005961; Phe-4-hydroxylase_tetra.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.800.10; Aaa_hydroxylase; 1.

PANTHER

PTHR11473; Aaa_hydroxylase; 1.

Pfam

PF01842; ACT; 1.
PF00351; Biopterin_H; 1.
Pfam graphical view of domain structure.

PRINTS

PR00372; FYWHYDRXLASE.

ProDom

PD002559; Aaa_hydroxylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01268; Phe4hydrox_tetr; 1.

PROSITE

PS00367; BIOPTERIN_HYDROXYL; 1.

Genome annotation databases

Ensembl

ENSRNOG00000004302; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P04176; -.

Other

UniRef

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

Keywords

3D-structure; Acetylation; Allosteric enzyme; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phenylalanine catabolism; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 453`	`452`	`Phenylalanine-4-hydroxylase.`	`PRO_0000205550`
`DOMAIN`	`36 111`	`76`	`ACT.`
`METAL`	`285 285`		`Iron.`
`METAL`	`290 290`		`Iron.`
`METAL`	`330 330`		`Iron.`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`16 16`		`Phosphoserine; by PKA.`
`STRAND`	`35 42`	`8`
`HELIX`	`47 56`	`10`
`TURN`	`57 59`	`3`
`STRAND`	`64 69`	`6`
`STRAND`	`76 81`	`6`
`HELIX`	`85 87`	`3`
`HELIX`	`88 100`	`13`
`STRAND`	`106 110`	`5`
`HELIX`	`125 129`	`5`
`TURN`	`130 133`	`4`
`TURN`	`147 150`	`4`
`HELIX`	`152 166`	`15`
`HELIX`	`181 201`	`21`
`HELIX`	`204 216`	`13`
`HELIX`	`227 238`	`12`
`STRAND`	`241 244`	`4`
`HELIX`	`251 258`	`8`
`TURN`	`259 261`	`3`
`STRAND`	`262 265`	`4`
`HELIX`	`283 289`	`7`
`HELIX`	`291 294`	`4`
`HELIX`	`297 310`	`14`
`HELIX`	`315 326`	`12`
`TURN`	`327 331`	`5`
`STRAND`	`333 336`	`4`
`STRAND`	`339 342`	`4`
`HELIX`	`345 348`	`4`
`HELIX`	`351 357`	`7`
`STRAND`	`359 366`	`8`
`HELIX`	`369 372`	`4`
`STRAND`	`379 382`	`4`
`STRAND`	`384 390`	`7`
`HELIX`	`392 403`	`12`
`STRAND`	`409 415`	`7`
`TURN`	`416 419`	`4`
`STRAND`	`420 424`	`5`

Sequence information

Length: 453 AA [This is the length of the unprocessed precursor]

Molecular weight: 51822 Da [This is the MW of the unprocessed precursor]

CRC64: 365D9E8A7E498D52 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVVLENGV LSRKLSDFGQ ETSYIEDNSN QNGAISLIFS LKEEVGALAK VLRLFEENDI 

        70         80         90        100        110        120 
NLTHIESRPS RLNKDEYEFF TYLDKRTKPV LGSIIKSLRN DIGATVHELS RDKEKNTVPW 

       130        140        150        160        170        180 
FPRTIQELDR FANQILSYGA ELDADHPGFK DPVYRARRKQ FADIAYNYRH GQPIPRVEYT 

       190        200        210        220        230        240 
EEEKQTWGTV FRTLKALYKT HACYEHNHIF PLLEKYCGFR EDNIPQLEDV SQFLQTCTGF 

       250        260        270        280        290        300 
RLRPVAGLLS SRDFLGGLAF RVFHCTQYIR HGSKPMYTPE PDICHELLGH VPLFSDRSFA 

       310        320        330        340        350        360 
QFSQEIGLAS LGAPDEYIEK LATIYWFTVE FGLCKEGDSI KAYGAGLLSS FGELQYCLSD 

       370        380        390        400        410        420 
KPKLLPLELE KTACQEYSVT EFQPLYYVAE SFSDAKEKVR TFAATIPRPF SVRYDPYTQR 

       430        440        450 
VEVLDNTQQL KILADSINSE VGILCNALQK IKS

P04176 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