[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C57BL/6J; TISSUE=Liver; PubMed=2334400 [NCBI, ExPASy, EBI, Israel, Japan] Ledley F.D., Grenett H.E., Dunbar B.S., Woo S.L.C.; "Mouse phenylalanine hydroxylase. Homology and divergence from human phenylalanine hydroxylase."; Biochem. J. 267:399-406(1990).
[2]	PROTEIN SEQUENCE OF 2-13; 54-68; 160-169 AND 253-261, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. STRAIN=C57BL/6; TISSUE=Liver; Bienvenut W.V.; Submitted (JUL-2005) to UniProtKB.
[3]	PROTEIN SEQUENCE OF 12-21. 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).
[4]	PROTEIN SEQUENCE OF 277-294. 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).
[5]	VARIANTS PAH-ENU1 ALA-106 AND PAH-ENU2 SER-263. DOI=10.1006/geno.1996.4508; PubMed=9119379 [NCBI, ExPASy, EBI, Israel, Japan] McDonald J.D., Charlton C.K.; "Characterization of mutations at the mouse phenylalanine hydroxylase locus."; Genomics 39:402-405(1997).

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.
DISEASE: Mouse strains deficient in phenylalanine hydroxylase (Pah) were created as models of phenylketonuria (PKU).
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

X51942; CAA36205.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15758; S15758.

UniGene

Mm.263539

3D structure databases

HSSP

P00439; 2PAH. [HSSP ENTRY / PDB]

SMR

P16331; 18-426, 19-427.

ModBase

P16331.

PTM databases

PhosphoSite

P16331; -.

Organism-specific databases

MGI

MGI:97473; Pah.

Gene expression databases

ArrayExpress

P16331; -.

CleanEx

MM_PAH; -.

GermOnline

ENSMUSG00000020051; Mus musculus.

Ontologies

GO:0004505;	Molecular function: phenylalanine 4-monooxygenase activity (inferred from mutant phenotype from MGI).
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

ENSMUSG00000020051; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

P16331; -.

HOVERGEN

P16331; -.

Other

SOURCE

Pah; Mus musculus.

UniRef

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

Keywords

Acetylation; Allosteric enzyme; Direct protein sequencing; Disease mutation; 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.`
`CHAIN`	`2 453`	`452`	`Phenylalanine-4-hydroxylase.`	`PRO_0000205549`
`DOMAIN`	`36 111`	`76`	`ACT.`
`METAL`	`285 285`		`Iron (By similarity).`
`METAL`	`290 290`		`Iron (By similarity).`
`METAL`	`330 330`		`Iron (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`MOD_RES`	`16 16`		`Phosphoserine; by PKA (By similarity).`
`VARIANT`	`106 106`	`1`	`V -> A (in PAH-ENU1; mild PKU phenotype).`
`VARIANT`	`263 263`	`1`	`F -> S (in PAH-ENU2; severe PKU phenotype).`

Sequence information

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

Molecular weight: 51929 Da [This is the MW of the unprocessed precursor]

CRC64: FA1CD4D0A598E8D9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVVLENGV LSRKLSDFGQ ETSYIEDNSN QNGAVSLIFS LKEEVGALAK VLRLFEENEI 

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

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

       190        200        210        220        230        240 
EEERKTWGTV 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 KTACQEYTVT EFRPLYYVAE SFNDAKEKVR TFAATIPRPF SVRYDPYTQR 

       430        440        450 
VEVLDNTQQL KNLADSINSE VGILCHALQK IKS

P16331 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