ID   DDC_DROSI               Reviewed;         510 AA.
AC   O96567; Q7Z0D9; Q7Z0E0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 100.
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;
GN   Name=Ddc;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND FUNCTION.
RC   TISSUE=Brain, and Epidermis;
RX   PubMed=12881721; DOI=10.1038/ng1218;
RA   De Luca M., Roshina N.V., Geiger-Thornsberry G.L., Lyman R.F.,
RA   Pasyukova E.G., Mackay T.F.C.;
RT   "Dopa decarboxylase (Ddc) affects variation in Drosophila longevity.";
RL   Nat. Genet. 34:429-433(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-510.
RC   STRAIN=St. Lucia;
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. Variation in the synthesis of bioamines may be a factor
CC       contributing to natural variation in individual life span.
CC       {ECO:0000269|PubMed:12881721}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Brain, 56.7 kDa;
CC         IsoId=O96567-1; Sequence=Displayed;
CC       Name=2; Synonyms=Hypoderm, 56.2 kDa;
CC         IsoId=O96567-2; Sequence=VSP_009723;
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AY197770; AAO16859.1; -; Genomic_DNA.
DR   EMBL; AY197770; AAO16860.1; -; Genomic_DNA.
DR   EMBL; AF091327; AAC67580.1; -; Genomic_DNA.
DR   AlphaFoldDB; O96567; -.
DR   SMR; O96567; -.
DR   ChiTaRS; Ddc; fly.
DR   GO; GO:0036467; F:5-hydroxy-L-tryptophan decarboxylase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0036468; F:L-dopa decarboxylase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0048085; P:adult chitin-containing cuticle pigmentation; IEA:EnsemblMetazoa.
DR   GO; GO:0007615; P:anesthesia-resistant memory; IEA:EnsemblMetazoa.
DR   GO; GO:0006585; P:dopamine biosynthetic process from tyrosine; IEA:EnsemblMetazoa.
DR   GO; GO:0007616; P:long-term memory; IEA:EnsemblMetazoa.
DR   GO; GO:0048082; P:regulation of adult chitin-containing cuticle pigmentation; IEA:EnsemblMetazoa.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:EnsemblMetazoa.
DR   GO; GO:0009611; P:response to wounding; IEA:EnsemblMetazoa.
DR   GO; GO:0006587; P:serotonin biosynthetic process from tryptophan; IEA:EnsemblMetazoa.
DR   GO; GO:0040040; P:thermosensory behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0043052; P:thermotaxis; IEA:EnsemblMetazoa.
DR   GO; GO:0035220; P:wing disc development; IEA:EnsemblMetazoa.
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   Alternative splicing; Catecholamine biosynthesis; Decarboxylase; Lyase;
KW   Pyridoxal phosphate.
FT   CHAIN           1..510
FT                   /note="Aromatic-L-amino-acid decarboxylase"
FT                   /id="PRO_0000146947"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         337
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..33
FT                   /note="MSHIPISNTIPPKQTDGNGKANISPDKLDPKVS -> MSIGLGTHIGVDNYA
FT                   RMLTKYFCIHIK (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_009723"
FT   CONFLICT        169
FT                   /note="V -> A (in Ref. 2; AAC67580)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  57312 MW;  46EFB646F1E5B116 CRC64;
     MSHIPISNTI PPKQTDGNGK ANISPDKLDP KVSIDMEAPE FKDFAKTMVD FIAEYLENIR
     DRRVLPEVKP GYLKPLIPDA APEKPEKWQD VMQDIERVIM PGVTHWHSPK FHAYFPTANS
     YPAIVADMLS GAIACIGFTW IASPACTELE VVMMDWLGKM LELPAEFLVC SGGKGGGVIQ
     GTASESTLVA LLGAKAKKLK EVKELHPEWD EHTILGKLVG YCSDQAHSSV ERAGLLGGVK
     LRSVQSENHR MRGAALEKAI EQDLAEGLIP FYAVVTLGTT NSCAFDYLDE CGPVGNKHNL
     WIHVDAAYAG SAFICPEYRH LMKGIESADS FNFNPHKWML VNFDCSAMWL KDPSWVVNAF
     NVDPLYLKHD MQGSAPDYRH WQIPLGRRFR ALKLWFVLRL YGVENLQAHI RRHCNFAKQF
     GDLCVADSRF ELAAEINMGL VCFRLKGSNE RNEALLKRIN GRGHIHLVPA KIKDVYFLRM
     AICSRFTQSE DMEYSWKEVS AAADEMEQEQ