ID   O44283_9NEOP            Unreviewed;       350 AA.
AC   O44283;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 83.
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   Hyalophora gloveri.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Saturniidae; Saturniinae; Attacini; Hyalophora.
OX   NCBI_TaxID=63986 {ECO:0000313|EMBL:AAC47884.1};
RN   [1] {ECO:0000313|EMBL:AAC47884.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9479702; DOI=10.1006/mpev.1997.9999;
RA   Friedlander T.P., Horst K.R., Regier J.C., Mitter C., Peigler R.S.,
RA   Fang Q.Q.;
RT   "Two nuclear genes yield concordant relationships within Attacini
RT   (Lepidoptera: Saturniidae).";
RL   Mol. Phylogenet. Evol. 9:131-140(1998).
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; AF015058; AAC47884.1; -; mRNA.
DR   AlphaFoldDB; O44283; -.
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:AAC47884.1"
FT   NON_TER         350
FT                   /evidence="ECO:0000313|EMBL:AAC47884.1"
SQ   SEQUENCE   350 AA;  39726 MW;  D0D2C21C89E6B3B5 CRC64;
     SSPACTELEV VMMDWLGQML ALPEEFLAKS GGEGGGVIQG TASEATLVAL LGAKAKITQR
     VKEQHPEWTD YEILSKLVGY ANKQAHSSVE RAGLLGGIKF RSLQPASDRR LNGEILREAM
     DEDIRNGLIP FYVVATLGTT ASCVFDDLDS IGDVCKERDI WLHVDAAYAG SAFVCPEYRY
     LMKGIEKADS FNFNPHKWLL VNFDCSALWL KQPRWIVDAF NVDPLYLKHD QQGSAPDYRH
     WQIPLGRRFR ALKLWFVLRL YGIENLQKHI RKQIALAHLF EKLCSSDERF EIFEEVTMGL
     VCFRLKGGNE INEELLRRIN GRGKIHLVPS KIDDVYFLRL AICSRMSEES
//