ID   B9U784_9NEOP            Unreviewed;       240 AA.
AC   B9U784;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 44.
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:ACD01619.1};
OS   Marumba quercus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Smerinthinae; Smerinthini; Marumba.
OX   NCBI_TaxID=522842 {ECO:0000313|EMBL:ACD01619.1};
RN   [1] {ECO:0000313|EMBL:ACD01619.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AToL-Lep-ID IJK-02-0118 {ECO:0000313|EMBL:ACD01619.1};
RX   PubMed=19492095; DOI=10.1371/journal.pone.0005719;
RA   Kawahara A.Y., Mignault A.A., Regier J.C., Kitching I.J., Mitter C.;
RT   "Phylogeny and biogeography of hawkmoths (Lepidoptera: Sphingidae):
RT   evidence from five nuclear genes.";
RL   PLoS ONE 4:e5719-e5719(2009).
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; EU479189; ACD01619.1; -; mRNA.
DR   AlphaFoldDB; B9U784; -.
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; 3.40.640.10; 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; 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         193
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACD01619.1"
FT   NON_TER         240
FT                   /evidence="ECO:0000313|EMBL:ACD01619.1"
SQ   SEQUENCE   240 AA;  26854 MW;  3326A4525CBCCC76 CRC64;
     CTELEVVMLD WLGQMLGLPE EFLARSGGEA GGVIQGTASE ATLVALLGAK SRTMHRVKEQ
     HPEWSETDIL GKLVGYCNQQ AHSSVERAGL LGGVTLRSLK PDSKRRLRGD TLREAIDEDI
     RNGLIPFYVV ATLGTTSSCA FDALDEIGDV CNSRDIWLHV DAAYAGSAFI CPEYRHYMKG
     VEKAESFNFN PHKWMLVNFD CSAMWLKQPR WIVDAFNVDP LYLKHDQQGA APDYRHWQIP
//