ID   D5FG45_DROMS            Unreviewed;       368 AA.
AC   D5FG45;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 38.
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:ACC68248.1};
OS   Drosophila mediostriata (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7269 {ECO:0000313|EMBL:ACC68248.1};
RN   [1] {ECO:0000313|EMBL:ACC68248.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20376692; DOI=10.1007/s10709-010-9453-0;
RA   Robe L.J., Valente V.L., Loreto E.L.;
RT   "Phylogenetic relationships and macro-evolutionary patterns within the
RT   Drosophila tripunctata "radiation" (Diptera: Drosophilidae).";
RL   Genetica 138:725-735(2010).
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; EU446067; ACC68248.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5FG45; -.
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   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; IPR015422; PyrdxlP-dep_Trfase_small.
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         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACC68248.1"
FT   NON_TER         368
FT                   /evidence="ECO:0000313|EMBL:ACC68248.1"
SQ   SEQUENCE   368 AA;  40827 MW;  078C22618BFED83A CRC64;
     WHSPKFHAYF PTANSYPAIV ADMLSGAIAC IGFTWIASPA RTELEVVMLD WLGKMLDLPA
     EFLACSGGKG GGVIQGTASE STLVALLGAK AKKLQEVKAE HPEWDEHTII GKLVGYTSAQ
     SHSSVERAGL LGGIKLRSVP ADEHNRLRGD ALEKAIQADL AEGLIPFYAV VTLGTTNSCA
     FDRLDECGPV ANKHNVWVHV DAAYAGSAFI CPEYRHHMKG IETADSFNFN PHKWMLVNFD
     CSAMWLKDPS WVVNAFNVDP LYLKHDMQGS APDYRHWQIP LGRRFRALKL WFVLRLYGVE
     NLQAHIRRHC GFAKQFADLC VADERFELAA EVNMGLVCFR LKGTNESNEA LLKRINGRGK
     IHMVPAKI
//