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 |
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PFAM accession number: | PF00351 |
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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:
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