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  Domain Name: pro_PheOH
Prokaryotic phenylalanine-4-hydroxylase (pro_PheOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes the eukaryotic proteins, phenylalanine-4-hydroxylase (eu_PheOH), tyrosine hydroxylase (TyrOH) and tryptophan hydroxylase (TrpOH). PheOH catalyzes the hydroxylation of L-Phe to L-tyrosine (L-Tyr). It uses (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) as the physiological electron donor.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 42
Total Disease Mutations Found: 42
This domain occurred 4 times on human genes (9 proteins).



  ATTENTION DEFICIT-HYPERACTIVITY DISORDER, SUSCEPTIBILITY TO, 7
  BIPOLAR AFFECTIVE DISORDER, SUSCEPTIBILITY TO
  HYPERPHENYLALANINEMIA, NON-PKU
  HYPERPHENYLALANINEMIA, NON-PKU MILD
  PHENYLKETONURIA
  PHENYLKETONURIA, INCLUDED
  SEGAWA SYNDROME, AUTOSOMAL RECESSIVE


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
metal binding site
cofactor binding site














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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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