ID   DDC_DROLE               Reviewed;         403 AA.
AC   O96571;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Aromatic-L-amino-acid decarboxylase;
DE            Short=AADC;
DE            EC=4.1.1.28;
DE   AltName: Full=DOPA decarboxylase;
DE            Short=DDC;
DE   Flags: Fragment;
GN   Name=Ddc;
OS   Drosophila lebanonensis (Fruit fly) (Scaptodrosophila lebanonensis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Scaptodrosophila.
OX   NCBI_TaxID=7225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Beirut;
RX   PubMed=10231575; DOI=10.1016/s0378-1119(99)00096-7;
RA   Tatarenkov A., Saez A.G., Ayala F.J.;
RT   "A compact gene cluster in Drosophila: the unrelated Cs gene is compressed
RT   between duplicated amd and Ddc.";
RL   Gene 231:111-120(1999).
CC   -!- FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine
CC       (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan
CC       to tryptamine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504,
CC         ChEBI:CHEBI:59905; EC=4.1.1.28;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxy-L-tryptophan + H(+) = CO2 + serotonin;
CC         Xref=Rhea:RHEA:18533, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:58266, ChEBI:CHEBI:350546; EC=4.1.1.28;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF091329; AAC67585.1; -; Genomic_DNA.
DR   AlphaFoldDB; O96571; -.
DR   SMR; O96571; -.
DR   FlyBase; FBgn0025671; Dleb\Ddc.
DR   Proteomes; UP000504634; Unplaced.
DR   GO; GO:0036467; F:5-hydroxy-L-tryptophan decarboxylase activity; IEA:RHEA.
DR   GO; GO:0036468; F:L-dopa decarboxylase activity; IEA:RHEA.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Catecholamine biosynthesis; Decarboxylase; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           <1..403
FT                   /note="Aromatic-L-amino-acid decarboxylase"
FT                   /id="PRO_0000146946"
FT   BINDING         8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   403 AA;  45134 MW;  558EB9B284D5D283 CRC64;
     KFHAYFPTAN SYPAIVADML SGAIACIGFT WIASPACTEL EVAMLDWLGK MLELPAEFLA
     CSGGKGGGVI QGTASEATLV ALLGAKAKKM KEVRETHPDW DDHTIISKLV GYSSAQAHSS
     VERAGLLGGV KLRSVPADEQ NRLRGEALEK AIEQDLADGL IPFYAVVTLG TTNSCAFDRL
     DECGPVANKH NVWVHVDAAY AGSAFICPEY RHLMKGIETA DSFNFNPHKW MLVNFDCSAM
     WLKDPSWVVN AFNVDPLYLK HDMQGSAPDY RHWQIPIGRR FRALKLWFVL RLYGVENLQA
     HIRRHCTYAQ QFAELCVQDS RFELAAEVNM GLVCFRLKGS NERNEALLKR INGRGKIHLV
     PAKIRDVYFL RMAVCSRFTR PEDMEYSWQE VSAAADEEEQ QQK