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Database: UniProt
Entry: A0A093ENC0_TYTAL
LinkDB: A0A093ENC0_TYTAL
Original site: A0A093ENC0_TYTAL 
ID   A0A093ENC0_TYTAL        Unreviewed;       394 AA.
AC   A0A093ENC0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Tryptophan 5-hydroxylase 2 {ECO:0000256|ARBA:ARBA00040889};
DE   AltName: Full=Tryptophan 5-monooxygenase 2 {ECO:0000256|ARBA:ARBA00042662};
DE   Flags: Fragment;
GN   ORFNames=N341_03802 {ECO:0000313|EMBL:KFV44897.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV44897.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV44897.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV44897.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KK373700; KFV44897.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093ENC0; -.
DR   Proteomes; UP000054190; Unassembled WGS sequence.
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   CDD; cd03346; eu_TrpOH; 1.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR036951; ArAA_hydroxylase_sf.
DR   InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR041904; TrpOH_cat.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF16; TRYPTOPHAN 5-HYDROXYLASE 2; 1.
DR   Pfam; PF00351; Biopterin_H; 2.
DR   PIRSF; PIRSF000336; TH; 2.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000336-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000336-1};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054190}.
FT   DOMAIN          1..56
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          62..394
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         205
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         227
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         235
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         242
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         247
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         287
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         306
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         316
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV44897.1"
FT   NON_TER         394
FT                   /evidence="ECO:0000313|EMBL:KFV44897.1"
SQ   SEQUENCE   394 AA;  45537 MW;  0D5B9008C6D17751 CRC64;
     QEKHVSMVHI ESRKSKRRNS EVEIFVDCDC SKKEFNELIQ LLKFQTNILS LNPPENIWTD
     EEGKAAFVTL DLDCVPWFPR KISELDKCSQ RVLMYGSELD ADHPGFKDNV YRQRRKYFVD
     VAMSYRYGQP IPRVEYTAEE IKTWGVVFRE LSKLYPTHAC REYLKNFPLL TKYCGYREDN
     VPQLEDVSIF LKERSGFTVR PVAGYLSPRD FLAGLAYRVF HCTQYIRHGS DPLYTPEPDT
     CHELLGHVPL LADPKFAQFS QEIGLASLGA SDEDVQKLAT CYFFTIEFGL CKQEGQLRAY
     GAGLLSSIGE LKECLITTFQ EAYFVSESFE EAKEKMRDFA KSINRPFSVY FNPYTQSIEI
     LKDTRSIENV VQDLRSDLNT VCDALSKMNR YLGI
//
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