ID   L7QR71_9NEOP            Unreviewed;       313 AA.
AC   L7QR71;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   Edosa sp. Edos.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tineoidea;
OC   Tineidae; Tineinae; Edosa.
OX   NCBI_TaxID=1181348 {ECO:0000313|EMBL:AGB87640.1};
RN   [1] {ECO:0000313|EMBL:AGB87640.1}
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:AGB87640.1}
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; JQ785830; AGB87640.1; -; mRNA.
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:AGB87640.1"
FT   NON_TER         313
FT                   /evidence="ECO:0000313|EMBL:AGB87640.1"
SQ   SEQUENCE   313 AA;  34606 MW;  DF1A144258D52DFB CRC64;
     VPAVKPGYLR PLVPEQAPQQ GEPWTAVMAD IERVVMSGVT HWHSPRFHAY FPTANSYPAI
     VADMLSGAIA CIGFTWIASP ACTELEVVML DWLGQMLGLP EXFLARSGGE AGGVIQGTAS
     EATLVALLGA KNKTIFRLKE QHPEWSENEI ISKLVGYCNK QAHSSVERAG LLGGVKLRNL
     APDSKRRLRG DTLKEAIEED KRNGLIPFYV VATLGTTSSC AFDVLEEIGQ VCKDEDVWLH
     VDAAYAGSAF ICPEYRYLMK GIELVDSFNF NPHKWMLVNF DCSAMWLKEP RWVVDAFNVD
     PLYLKHDQQG SAP
//