ID   Q8T786_9NEOP            Unreviewed;       350 AA.
AC   Q8T786;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 66.
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;
OS   Calosaturnia walterorum.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Saturniidae; Saturniinae; Saturniini; Calosaturnia.
OX   NCBI_TaxID=180238 {ECO:0000313|EMBL:AAM18859.1};
RN   [1] {ECO:0000313|EMBL:AAM18859.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Regier J.C., Mitter C., Peigler R.S., Friedlander T.P.;
RT   "Monophyly, composition, and relationships within Saturniinae (Lepidoptera:
RT   Saturniidae): Evidence from two nuclear genes.";
RL   Insect Syst. Evol. 0:0-0(2002).
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; AF373975; AAM18859.1; -; mRNA.
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   2: Evidence at transcript level;
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         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAM18859.1"
FT   NON_TER         350
FT                   /evidence="ECO:0000313|EMBL:AAM18859.1"
SQ   SEQUENCE   350 AA;  39749 MW;  820FB33C2E2233D1 CRC64;
     SSPACTELEV VMLDWLGQML GLPEEFLAKS GGEGGGVIQG TASEATLVAL LGAKARITQR
     VKEQHPEWTE YEILSKLVGY ANKQAHSSVE RAGLLGGIKF RSLQPGSDRR LNGEILREAM
     DEXIRNGLIP FYVVVTLGTT SSCVFDDLDG IGDICKSRDI WLHVDAAYAG SAFICPEYRY
     LMKGIEKADS FNFNPHKWLL VNFDCSAMWL KQPRWIVDAF NVDPLYLKHD QQGSAPDYRH
     WQIPLGRRFR ALKLWFVLRL YGVENLQKHI RKQIALAHLF EKLCNSDERF EIFEEVTMGL
     VCFRLKGGNE INEELLRRIN GRGKIHLVPS KIDDVYFLRL AICSRMSEES
//