[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=Testis; NIH - Mammalian Gene Collection (MGC) project; Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: L-phenylalanine + tetrahydrobiopterin + O₂ = L-tyrosine + 4a-hydroxytetrahydrobiopterin.
COFACTOR: Fe(2+) ion (By similarity).
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 (By similarity).
PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid and fumarate from L-phenylalanine: step 1/6 .
SUBUNIT: Homodimer (By similarity).
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

BT030585; ABQ13025.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112633; AAI12634.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001039523.1; -.

UniGene

Bt.61435

3D structure databases

SMR

Q2KIH7; 19-426.

ModBase

Q2KIH7.

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.

BLOCKS

Q2KIH7.

Genome annotation databases

Ensembl

ENSBTAG00000012794; Bos taurus. [Contig view]

GeneID

510583; -.

KEGG

bta:510583; -.

Phylogenomic databases

HOVERGEN

Q2KIH7; -.

Other

ProtoNet

Q2KIH7.

UniRef

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

Keywords

Allosteric enzyme; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phenylalanine catabolism; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 451`	`451`	`Phenylalanine-4-hydroxylase.`	`PRO_0000281913`
`DOMAIN`	`34 109`	`76`	`ACT.`
`METAL`	`284 284`		`Iron (By similarity).`
`METAL`	`289 289`		`Iron (By similarity).`
`METAL`	`329 329`		`Iron (By similarity).`
`MOD_RES`	`16 16`		`Phosphoserine; by PKA (By similarity).`

Sequence information

Length: 451 AA [This is the length of the unprocessed precursor]

Molecular weight: 51727 Da [This is the MW of the unprocessed precursor]

CRC64: 2D2791910652BD2E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSALVLESRA LGRKLSDFGQ ETSYIEGNSD QNAVSLIFSL KEEVGALARV LRLFEENDIN 

        70         80         90        100        110        120 
LTHIESRPSR LRKDEYEFFT NLDQRSVPAL ANIIKILRHD IGATVHELSR DKKKDTVPWF 

       130        140        150        160        170        180 
PRTIQELDNF ANQVLSYGAE LDADHPGFKD PVYRARRKQF ADIAYNYRHG QPIPRVEYTE 

       190        200        210        220        230        240 
EEKKTWGTVF RTLKSLYKTH ACYEHNHIFP LLEKYCGFRE DNIPQLEEVS QFLQSCTGFR 

       250        260        270        280        290        300 
LRPVAGLLSS RDFLGGLAFR VFHCTQYIRH GSKPMYTPEP DICHELLGHV PLFSDRSFAQ 

       310        320        330        340        350        360 
FSQEIGLASL GAPDEYIEKL ATIYWFTVEF GLCKQGDSIK AYGAGLLSSF GELQYCLSDK 

       370        380        390        400        410        420 
PKLLPLELEK TAVQEYTITE FQPLYYVAES FNDAKEKVRN FAATIPRPFS VHYDPYTQRI 

       430        440        450 
EVLDNTQQLK ILADSISSEV EILCSALQKL K

Q2KIH7 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