ID   L7QQV1_9NEOP            Unreviewed;       313 AA.
AC   L7QQV1;
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   Aroga trialbamaculella.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Gelechioidea;
OC   Gelechiidae; Gelechiinae; Aroga.
OX   NCBI_TaxID=1178187 {ECO:0000313|EMBL:AGB87500.1};
RN   [1] {ECO:0000313|EMBL:AGB87500.1}
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:AGB87500.1}
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; JQ785690; AGB87500.1; -; mRNA.
DR   AlphaFoldDB; L7QQV1; -.
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; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
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         274
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGB87500.1"
FT   NON_TER         313
FT                   /evidence="ECO:0000313|EMBL:AGB87500.1"
SQ   SEQUENCE   313 AA;  34575 MW;  38C8FF719BE44A63 CRC64;
     VPSVKPGYLR PLVPEKAPEK AEPWTAVMAD IERVVMSGVT HWHSPRFHAY FPTAQSYPAI
     VADMLSGAIA CIGFTWIASP ACTELEVVML DWLGQMLGLP EEFLARSGGE GGGVIQGTAS
     EATLVALLGA KSRMMVRVKE QHPEWTENDI LAKLVGYCSK QAHSSVERAG LLGGVTLRGV
     KPDSKRQLRG DLLRDAIEED LRNGLIPFYV VATLGTTSSC TFDNLDEIGD VCREYGIWLH
     VDAAYAGSAF ICPEYRYLMK GIEKADSFDF NPHKWLLVNF DCSAMWLKEP RWIVDAFNVD
     PLYLKHDQQG SAP
//