ID   Q58H42_9NEOP            Unreviewed;       321 AA.
AC   Q58H42;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 55.
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:AAX54956.1};
OS   Abrostola asclepiadis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Plusiinae; Abrostola.
OX   NCBI_TaxID=319803 {ECO:0000313|EMBL:AAX54956.1};
RN   [1] {ECO:0000313|EMBL:AAX54956.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mitchell A., Mitter C., Regier J.C.;
RT   "Systematics and evolution of the cutworm moths (Lepidoptera: Noctuidae):
RT   evidence from two protein-coding nuclear genes.";
RL   Syst. Entomol. 31:21-46(2005).
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; AY952519; AAX54956.1; -; mRNA.
DR   AlphaFoldDB; Q58H42; -.
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   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         178
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAX54956.1"
FT   NON_TER         321
FT                   /evidence="ECO:0000313|EMBL:AAX54956.1"
SQ   SEQUENCE   321 AA;  36360 MW;  E0D049C8E26DA45B CRC64;
     LGLPDSFLAR SGGEAGGVIQ GTASEATLVA LLGAKSRTMQ RVKEQHPEWT ETEILSKLVG
     YCNKQAHSSV ERAGLLGGVK LRSLKPDGKR RLRGETLQEA IDEDLRNGLI PFYVVATLGT
     TSSCSFDALD EIGDVCNALD IWLHVDAAYA GSAFICPEYR YLMKGAEKAS SFNFNPHKWL
     LVNFDCSAMW LKEPRWIVDA FNVDPLYLKH DQQGSAPDYR HWQIPLGRRF RALKLWFVLR
     LYGVENLQKH IRKHIGLAHL FERLCSADER FEIFEEVIMG LVCFRLKGGN EQNEELLRRI
     NGRGKIHLVP SIIDDTYFLR L
//