ID   O01951_9NEOP            Unreviewed;       230 AA.
AC   O01951;
DT   01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 80.
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;
GN   Name=DDC {ECO:0000313|EMBL:AAB58078.1};
OS   Australothis rubrescens.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Australothis.
OX   NCBI_TaxID=52343 {ECO:0000313|EMBL:AAB58078.1};
RN   [1] {ECO:0000313|EMBL:AAB58078.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Australia {ECO:0000313|EMBL:AAB58078.1};
RX   PubMed=11975343;
RA   Fang Q.Q., Cho S., Regier J.C., Mitter C., Matthews M., Poole R.W.,
RA   Friedlander T.P., Zhao S.;
RT   "A new nuclear gene for insect phylogenetics: dopa decarboxylase is
RT   informative of relationships within Heliothinae (Lepidoptera: Noctuidae).";
RL   Syst. Biol. 46:269-283(1997).
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; U71409; AAB58078.1; -; Genomic_DNA.
DR   AlphaFoldDB; O01951; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
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         190
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAB58078.1"
FT   NON_TER         230
FT                   /evidence="ECO:0000313|EMBL:AAB58078.1"
SQ   SEQUENCE   230 AA;  25566 MW;  7F2774EA0BEAAB11 CRC64;
     LEVVMLDWLG QMLGLPESFL ARSGGEAGGV IQGTASEATL VALLGAKNRT IVRVKEQHPE
     WTDIEIVSKL VGYCNKQAHS SVERAGLLGG VKLRSLKPDE KRRLRGETLQ EAIEEDIRNG
     LIPFYVVATL GTTSSCAFDA LDEIGDVCSK HEIWLHVDAA YAGSAFICPE YRYLMKGVEK
     ADSFNFNPHK WMLVNFDCSA MWLKQPRWIV DAFNVDPLYL KHDQQGSAPD
//