ID   Q7YSL8_9MUSC            Unreviewed;       281 AA.
AC   Q7YSL8;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 77.
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;
GN   Name=Ddc {ECO:0000313|EMBL:AAM80963.1,
GN   ECO:0000313|FlyBase:FBgn0067287};
OS   Drosophila antillea.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=133984 {ECO:0000313|EMBL:AAM80963.1};
RN   [1] {ECO:0000313|EMBL:AAM80963.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BD I {ECO:0000313|EMBL:AAM80965.1}, MGM III
RC   {ECO:0000313|EMBL:AAM80964.1}, and MT V {ECO:0000313|EMBL:AAM80963.1};
RA   Wilder J.A., Dyreson E., Spangler M.L., Sainz A.H., Hollocher H.;
RT   "Molecular Footprints of Natural Selection on Pigmentation Genes in the
RT   Drosophila dunni Subgroup.";
RL   Submitted (JUN-2002) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY126905; AAM80963.1; -; Genomic_DNA.
DR   EMBL; AY126906; AAM80964.1; -; Genomic_DNA.
DR   EMBL; AY126907; AAM80965.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7YSL8; -.
DR   FlyBase; FBgn0067287; Dant\Ddc.
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   3: Inferred from homology;
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         179
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAM80963.1"
FT   NON_TER         281
FT                   /evidence="ECO:0000313|EMBL:AAM80963.1"
SQ   SEQUENCE   281 AA;  31232 MW;  AA1E5643CE7C3840 CRC64;
     MLDLPAEFLA CSGGKGGGVI QGTASESTLV ALLGAKAKKL QEVKAEHPEW DDHTIIGKLV
     GYTSAQSHSS VERAGLLGGI KLRSVPADEH NRLRGDALEK AIEKDLAEGL IPFYAVVTLG
     TTNSCAFDRL DECGPVANKH KVWVHVDAAY AGSAFICPEY RHHMKGIETA DSFNFNPHKW
     MLVNFDCSAM WLKDPSWVVN AFNVDPLYLK HDMQGSAPDY RHWQIPLGRR FRALKLWFVL
     RLYGVENLQA HIRRHCGFAQ QFADLCVADE RFELAAEVNM G
//