The domain within your query sequence starts at position 165 and ends at position 232; the E-value for the Biopterin_H domain shown below is 7.2e-37.



PFAM accession number:PF00351
Interpro abstract (IPR019774):

Hydroxylation of the aromatic amino acids phenylalanine, tyrosine and tryptophan is carried out by a family of non-heme iron and tetrahydrobiopterin (BH4) dependent enzymes: the aromatic amino acid hydroxylase [ (PUBMED:3475690) ]. Theseenzymes are structurally and functionally similar. The eukaryotic forms include a regulatory N-terminal domain, a catalytic domain and a C-terminal oligomerization motif. The eukaryotic enzymes are all homotetramers [ (PUBMED:14640675) (PUBMED:15537351) ].

Three-dimensional structures have been determined for the three types of enzymes. The iron atom is bound to three amino acid residues, two close histidine and a more distant acidic residue. This arrangement of ligands has been observed in a number of metalloproteins with divergent function [ (PUBMED:11718561) ].

Enzymes that belong to the aromatic amino acid hydroxylase family are listed below:

  • Phenylalanine-4-hydroxylase ( EC ) (PAH). Catalyzes the conversion of phenylalanine to tyrosine. In humans, deficiencies [ (PUBMED:8594560) ] of PAH are the cause of phenylketonuria, the most common inborn error of amino acid metabolism. In the bacteria Chromobacterium violaceum [ (PUBMED:1655752) ], PAH is copper-dependent; it is iron-dependent in Pseudomonas aeruginosa [ (PUBMED:8108417) ].
  • Tyrosine 3-hydroxylase ( EC ) (TYH). Catalyzes the rate limiting step in catecholamine biosynthesis: the conversion of tyrosine to 3,4- dihydroxy-L-phenylalanine.
  • Tryptophan 5-hydroxylase ( EC ) (TRH). Catalyzes the rate-limiting step in serotonin biosynthesis: the conversion of tryptophan to 3-hydroxy- anthranilate.

This entry represents a domain containing the catalytic domain and the coiled-coil C-terminal oligomerization motif.

GO process:oxidation-reduction process (GO:0055114)
GO function:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen (GO:0016714)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Biopterin_H