P04176
uniprot
P04176
canonical
activity_regulation
ACTIVITY 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. {ECO:0000250|UniProtKB:P00439}.
uniprot
proteins
amino_acid_sequence
MAAVVLENGVLSRKLSDFGQETSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDINLTHIESRPSRLNKDEYEFFTYLDKRTKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKTACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSINSEVGILCNALQKIKS
uniprot
proteins
ec_number
1.14.16.1
uniprot
proteins
function
FUNCTION: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine. {ECO:0000250|UniProtKB:P00439}.
uniprot
proteins
mass_dalton
51822
uniprot
proteins
pathway_participation
PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine. {ECO:0000250|UniProtKB:P00439}.
uniprot
proteins
protein_family
Biopterin-dependent aromatic amino acid hydroxylase family
uniprot
proteins
pubmed
10331871
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2869038
uniprot
proteins
pubmed
6098294
uniprot
proteins
pubmed
7387651
uniprot
proteins
pubmed
7407194
uniprot
proteins
sequence_length
453
uniprot
proteins