ID   DDC_MANSE               Reviewed;         508 AA.
AC   P48861;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, 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;
GN   Name=Ddc;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Epidermis;
RX   PubMed=7750638; DOI=10.1006/dbio.1995.1137;
RA   Hiruma K., Carter M.S., Riddiford L.M.;
RT   "Characterization of the dopa decarboxylase gene of Manduca sexta and its
RT   suppression by 20-hydroxyecdysone.";
RL   Dev. Biol. 169:195-209(1995).
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; U03909; AAC46604.1; -; mRNA.
DR   AlphaFoldDB; P48861; -.
DR   SMR; P48861; -.
DR   BRENDA; 4.1.1.28; 3173.
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   2: Evidence at transcript level;
KW   Catecholamine biosynthesis; Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..508
FT                   /note="Aromatic-L-amino-acid decarboxylase"
FT                   /id="PRO_0000146948"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         303
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   508 AA;  57892 MW;  87538994956A7C77 CRC64;
     MNPGDFKDFA KAMTDYITEY LENIRDRQVV PSVKPGYLRP LVPEQAPQQA EPWTAVMADI
     ERVVMSGVTH WQSPRFHAYF PTANSYPSIV ADMLSGAIAC IGFTWIASPA CTELEVVMLD
     WLGQMLGLPD QFLARSGGEG GGVIQGTASE ATFVALLGAK SRMMHRVKEQ HPEWTETDIL
     GKLVGYCNQQ AHSSVERAGL LGGVKLRSLK PDSKRRLRGD TLREAIDEDI RNGLIPFYVV
     ATLGTTSSCA FDALDEIGDV CNASDIWLHV DAAYAGSAFI CPEYRHFMKG VEKADSFNFN
     PHKWMLVNFD CSAMWLKQPR WIVDAFNVDP LYLKHEQQGS APDYRHWQIP LGRRFRSLKL
     WFVLRLYGVE NLQKYIRKQI GFAHLFERLL TSDERFELFE EVTMGLVCFR LKGSNEINEE
     LLRRINGRGK IHLVPSKVDD VYFLRLAICS RFTEESDMHV SWEEIKDRLM MFLKSKGAVL
     IKIICSTTRR TKNILTYIKQ NIFRDVGL