ID   U3IEP2_ANAPP            Unreviewed;       343 AA.
AC   U3IEP2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 2.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Biopterin-dependent aromatic amino acid hydroxylase family profile domain-containing protein {ECO:0000259|PROSITE:PS51410};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000005714.2, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000005714.2, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000005714.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|PIRSR:PIRSR601273-2};
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}.
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DR   AlphaFoldDB; U3IEP2; -.
DR   Ensembl; ENSAPLT00000006346.2; ENSAPLP00000005714.2; ENSAPLG00000006128.2.
DR   GeneTree; ENSGT00950000182885; -.
DR   HOGENOM; CLU_023198_2_0_1; -.
DR   Proteomes; UP000016666; Chromosome 5.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016714; F: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; IEA:InterPro.
DR   GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR036951; ArAA_hydroxylase_sf.
DR   InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF23; TRYPTOPHAN 5-HYDROXYLASE 1; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601273-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601273-2};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016666}.
FT   DOMAIN          1..314
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         114
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         136
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         144
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         151
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         156
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         211
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         241
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
SQ   SEQUENCE   343 AA;  38748 MW;  D57A47C1CB8EBCF0 CRC64;
     IKPLSLKAFQ HVDQISLYIL WCSGLKPDQV RVLLSSSPFS GDPVPKIEFT EEEVKTWGTV
     YQELNKFYPA HACREYLKHL PLLKYCGYRE NNIPQLEDVS LFLKGFTIRL VVGYLSPRDF
     LVGLAFRVFH CTRYVRHGSD PLYTPEPDTC HELLGHISLL AEPSFAQFWE IGLASLGASN
     EAVQKLATVS VSFGLCKQEG QLRVYGASLL SSISGLKHLL SGSAKVKPLH PKVTCKQECL
     ITTFQEVYFV SESFEEAKEK MREFAKTIKH PFGMQYNPYT QSVQILKDTK SIASMVNELR
     HELDVVIDAL SKMGKQLEVK HSHHQCGVLS NSILFPADFF LGM
//