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Database: UniProt
Entry: A0A3Q0J7Q9_DIACI
LinkDB: A0A3Q0J7Q9_DIACI
Original site: A0A3Q0J7Q9_DIACI 
ID   A0A3Q0J7Q9_DIACI        Unreviewed;       379 AA.
AC   A0A3Q0J7Q9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Tryptophan 5-hydroxylase 1-like {ECO:0000313|RefSeq:XP_026684504.1};
GN   Name=LOC113470334 {ECO:0000313|RefSeq:XP_026684504.1};
OS   Diaphorina citri (Asian citrus psyllid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC   Diaphorininae; Diaphorina.
OX   NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_026684504.1};
RN   [1] {ECO:0000313|RefSeq:XP_026684504.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_026684504.1; XM_026828703.1.
DR   AlphaFoldDB; A0A3Q0J7Q9; -.
DR   SMR; A0A3Q0J7Q9; -.
DR   STRING; 121845.A0A3Q0J7Q9; -.
DR   PaxDb; 121845-A0A3Q0J7Q9; -.
DR   KEGG; dci:113470334; -.
DR   OrthoDB; 275463at2759; -.
DR   Proteomes; UP000079169; Unplaced.
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; 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   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF40; TRYPTOPHAN 5-MONOOXYGENASE; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 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: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:UP000079169}.
FT   DOMAIN          83..346
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         141
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         163
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         171
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         223
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         242
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT   BINDING         273
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
SQ   SEQUENCE   379 AA;  43292 MW;  480FD32E23478843 CRC64;
     MDQISLCVPD LRLRHRENPD FFYINKNLRS SYLHSTIPSG LMLYNKHSLD LDLSTAPRRF
     KEVCRTVLGG GRFPSGRTEE GVIFNELHKL YIKHACHEYL ENWPELVRYC GYREDNIPQL
     EDVNTYLKRK TGFQLRPVAG YLSPRDFLSG LAFRVFHCTQ YIRHSSDPFY TPEPDCCHEL
     LGHMPLLANP TFAQFSQELG LTSLGASDED VERLGTLYFF TVEFGLCKQD GALKVYGAGL
     LSSVAELTHA VTNAGDKIRR FDPAVTVSEE CIITAYQNAY YYTDSFEEAK EKMREFAGTI
     QRPFGVRYNP YTQSVEVLSN SEKIAALVSE LRGDLCIVRN ALKKIHAREE TVENLTHMLT
     DTMHINTQDE EEGQDISPN
//
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