ID   L7QTH0_9NEOP            Unreviewed;       313 AA.
AC   L7QTH0;
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   Pereute charops.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Pieridae; Pierinae; Pereute.
OX   NCBI_TaxID=320219 {ECO:0000313|EMBL:AGB87859.1};
RN   [1] {ECO:0000313|EMBL:AGB87859.1}
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:AGB87859.1}
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; JQ786049; AGB87859.1; -; mRNA.
DR   AlphaFoldDB; L7QTH0; -.
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:AGB87859.1"
FT   NON_TER         313
FT                   /evidence="ECO:0000313|EMBL:AGB87859.1"
SQ   SEQUENCE   313 AA;  34444 MW;  CF7DB9F2A1D40810 CRC64;
     VPSVKPGYLR PLVPEQAPEK PEPWTAVMAD IEQVVMSGVT HWHSPRFHAY FPTANSYPAI
     VADMLSGAIA CIGFSWIASP ACTELEVVML DWLGQMLGIP EEFLARSGGE GGGVIQGTAS
     EATLVALLGA KSKAMHRAKE QHPDWTDVEI LSKLVGYCNK QAHSSVERAG LLGGVKLRSL
     KPDNKRSLRG ETLQEAIKED IKNGLIPFFA VATLGTTSTC AFDNLDEIGD VCQESDIWLH
     IDAAYAGSSF ICPEYRYLMK GIEKADSFNF NPHKWLLVNF DCSAMWLKQP RWIVDAFNVD
     PLYLKYDQQG SAP
//