ID   L7QSD6_9NEOP            Unreviewed;       236 AA.
AC   L7QSD6;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000256|ARBA:ARBA00040968};
DE            EC=4.1.1.28 {ECO:0000256|ARBA:ARBA00038886};
DE   AltName: Full=DOPA decarboxylase {ECO:0000256|ARBA:ARBA00041275};
DE   Flags: Fragment;
OS   Anatrachyntis japonica.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Gelechioidea;
OC   Cosmopterigidae; Cosmopteriginae; Anatrachyntis.
OX   NCBI_TaxID=1178223 {ECO:0000313|EMBL:AGB87479.1};
RN   [1] {ECO:0000313|EMBL:AGB87479.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Regier J.C., Mitter C., Solis M.A., Hayden J.E., Landry B., Nuss M.,
RA   Simonsen T.J., Yen S.-H., Zwick A., Cummings M.P.;
RT   "A molecular phylogeny for the pyraloid moths (Lepidoptera: Pyraloidea) and
RT   its implications for higher-level classification.";
RL   Syst. Entomol. 37:635-656(2012).
RN   [2] {ECO:0000313|EMBL:AGB87479.1}
RP   NUCLEOTIDE SEQUENCE.
RG   LepTree.net;
RA   Regier J.C.;
RT   "Assembling the Tree of Life Lepidoptera.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; JQ785669; AGB87479.1; -; mRNA.
DR   AlphaFoldDB; L7QSD6; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGB87479.1"
FT   NON_TER         236
FT                   /evidence="ECO:0000313|EMBL:AGB87479.1"
SQ   SEQUENCE   236 AA;  26006 MW;  4547BDCA566C0F5A CRC64;
     ASPACTELEV VMLDWLGQML GLPDAFLAKS GGEGGGVIQG TASEATLVAL LGAKARTMQR
     VKEQHPEWTE TDILSKLVGY CSKQAHSSVE RAGLLGGVKL RSVKPDGKRR LRGDILREVI
     EEDIKNGLIP FYVVATLGTT SSCTFDALDE IGDVCNELNL WLHVDAAYAG SAFICPEYRY
     LMKGIEKADS FDFNPHKWLL VNFDCSAFWL KEPRWIVDAF NVDPLYLKHD MQGAVP
//