ID   PH4H_BOVIN              Reviewed;         451 AA.
AC   Q2KIH7; A5D9G6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Phenylalanine-4-hydroxylase;
DE            Short=PAH;
DE            EC=1.14.16.1;
DE   AltName: Full=Phe-4-monooxygenase;
GN   Name=PAH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-phenylalanine + tetrahydrobiopterin + O(2) =
CC       L-tyrosine + 4a-hydroxytetrahydrobiopterin.
CC   -!- COFACTOR: Fe(2+) ion (By similarity).
CC   -!- ENZYME REGULATION: N-terminal region of PAH is thought to contain
CC       allosteric binding sites for phenylalanine and to constitute an
CC       "inhibitory" domain that regulates the activity of a catalytic
CC       domain in the C-terminal portion of the molecule (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetic acid and fumarate from L-phenylalanine: step 1/6.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family.
CC   -!- SIMILARITY: Contains 1 ACT domain.
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DR   EMBL; BT030585; ABQ13025.1; -; mRNA.
DR   EMBL; BC112633; AAI12634.1; -; mRNA.
DR   IPI; IPI00685821; -.
DR   RefSeq; NP_001039523.1; -.
DR   UniGene; Bt.61435; -.
DR   SMR; Q2KIH7; 19-426.
DR   Ensembl; ENSBTAG00000012794; Bos taurus.
DR   GeneID; 510583; -.
DR   KEGG; bta:510583; -.
DR   HOVERGEN; Q2KIH7; -.
DR   OMA; Q2KIH7; QETSYIE.
DR   BRENDA; 1.14.16.1; 251.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:EC.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002912; ACT_bd.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR005961; Phe-4-hydroxylase_tetra.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   Gene3D; G3DSA:1.10.800.10; Aaa_hydroxylase; 1.
DR   PANTHER; PTHR11473; Aaa_hydroxylase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   ProDom; PD002559; Aaa_hydroxylase; 1.
DR   TIGRFAMs; TIGR01268; Phe4hydrox_tetr; 1.
DR   PROSITE; PS00367; BIOPTERIN_HYDROXYL; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Phenylalanine catabolism; Phosphoprotein.
FT   CHAIN         1    451       Phenylalanine-4-hydroxylase.
FT                                /FTId=PRO_0000281913.
FT   DOMAIN       34    109       ACT.
FT   METAL       284    284       Iron (By similarity).
FT   METAL       289    289       Iron (By similarity).
FT   METAL       329    329       Iron (By similarity).
FT   MOD_RES      16     16       Phosphoserine; by PKA (By similarity).
SQ   SEQUENCE   451 AA;  51727 MW;  2D2791910652BD2E CRC64;
     MSALVLESRA LGRKLSDFGQ ETSYIEGNSD QNAVSLIFSL KEEVGALARV LRLFEENDIN
     LTHIESRPSR LRKDEYEFFT NLDQRSVPAL ANIIKILRHD IGATVHELSR DKKKDTVPWF
     PRTIQELDNF ANQVLSYGAE LDADHPGFKD PVYRARRKQF ADIAYNYRHG QPIPRVEYTE
     EEKKTWGTVF RTLKSLYKTH ACYEHNHIFP LLEKYCGFRE DNIPQLEEVS QFLQSCTGFR
     LRPVAGLLSS RDFLGGLAFR VFHCTQYIRH GSKPMYTPEP DICHELLGHV PLFSDRSFAQ
     FSQEIGLASL GAPDEYIEKL ATIYWFTVEF GLCKQGDSIK AYGAGLLSSF GELQYCLSDK
     PKLLPLELEK TAVQEYTITE FQPLYYVAES FNDAKEKVRN FAATIPRPFS VHYDPYTQRI
     EVLDNTQQLK ILADSISSEV EILCSALQKL K
//