The domain within your query sequence starts at position 150 and ends at position 480; the E-value for the Biopterin_H domain shown below is 3.6e-177.

PWFPRKISELDRCSHRVLMYGTELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVE
YTEEETKTWGVVFRELSKLYPTHACREYLKNLPLLTKYCGYREDNVPQLEDVSMFLKERS
GFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPK
FAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHAL
SDKACVKSFDPKTTCLQECLITTFQDAYFVSDSFEEAKEKMRDFAKSITRPFSVYFNPYT
QSIEILKDTRSIENVVQDLRSDLNTVCDALN

Biopterin_H

Biopterin_H
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 1.14.16.1) (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 1.14.16.2) (TYH). Catalyzes the rate limiting step in catecholamine biosynthesis: the conversion of tyrosine to 3,4- dihydroxy-L-phenylalanine.
  • Tryptophan 5-hydroxylase (EC 1.14.16.4) (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