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Database: UniProt
Entry: B9U719_9NEOP
LinkDB: B9U719_9NEOP
Original site: B9U719_9NEOP 
ID   B9U719_9NEOP            Unreviewed;       350 AA.
AC   B9U719;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:ACD01554.1};
OS   Acosmeryx naga.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Macroglossinae; Macroglossini; Acosmeryx.
OX   NCBI_TaxID=522778 {ECO:0000313|EMBL:ACD01554.1};
RN   [1] {ECO:0000313|EMBL:ACD01554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AToL-Lep-ID AYK-04-2570 {ECO:0000313|EMBL:ACD01554.1};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; EU479124; ACD01554.1; -; mRNA.
DR   AlphaFoldDB; B9U719; -.
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   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:SF167; 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   Catecholamine biosynthesis {ECO:0000256|ARBA:ARBA00022584};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR602129-50}.
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:ACD01554.1"
FT   NON_TER         350
FT                   /evidence="ECO:0000313|EMBL:ACD01554.1"
SQ   SEQUENCE   350 AA;  39816 MW;  DFB79E5E2E70627A CRC64;
     ASPACTELEV VMLDWLGQML GLPEEFLARS GGEAGGVIQG TASEATLVAL LGAKSRMMQK
     LKEEHPEWSE TDILGKLVGY CNKQAHSSVE RAGLLGGVKL RSLQPDSKRR LRGDILREAM
     DEDISKGLIP FYVVATLGTT SSCTFDALDE IGDVCNSRNI WLHVDAAYAG SAFICPEYRY
     LMKGVEKADS FNFNPHKWML VNFDCSAMWL KQPRWIVDAF NVDPLYLKHD QQGSAPDYRH
     WQIPLGRRFR SLKLWFVLRL YGVENLQKHI RKQIALAHLF EKLLTEDERF ELFEEVTMGL
     VCFRLKGSNE INEELLRRIN GRGKIHLVPS KIDDVYFLRL AICSRFTEDS
//
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