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Database: UniProt
Entry: Q9Y0P3_9NEOP
LinkDB: Q9Y0P3_9NEOP
Original site: Q9Y0P3_9NEOP 
ID   Q9Y0P3_9NEOP            Unreviewed;       236 AA.
AC   Q9Y0P3;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 77.
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:AAD37656.1};
OS   Charadra deridens.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Pantheinae; Charadra.
OX   NCBI_TaxID=56378 {ECO:0000313|EMBL:AAD37656.1};
RN   [1] {ECO:0000313|EMBL:AAD37656.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12118405; DOI=10.1080/10635159950173816;
RA   Mitchell A., Mitter C., Regier J.C.;
RT   "More taxa or more characters revisited: combining data from nuclear
RT   protein-encoding genes for phylogenetic analyses of Noctuoidea (Insecta:
RT   Lepidoptera).";
RL   Syst. Biol. 49:202-224(2000).
RN   [2] {ECO:0000313|EMBL:AAD37656.1}
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   -!- 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; AF151573; AAD37656.1; -; mRNA.
DR   AlphaFoldDB; Q9Y0P3; -.
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   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: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:AAD37656.1"
FT   NON_TER         236
FT                   /evidence="ECO:0000313|EMBL:AAD37656.1"
SQ   SEQUENCE   236 AA;  26033 MW;  390E0E7A673DC918 CRC64;
     ASPACTELEV VMLDWLGQML GLPETFLARS GGEAGGVIQG TASEATLVAL LGAKSRMMTR
     VKEQHPEWTD TEILSKLVGY CNKQAHSSVE RAGLLGGVKL RSLQPDNKRR LRGDILKEAI
     EKDISDGLIP FYVVATLGTT SSCTFDALDE IGDVCNSFDL WLHVDAAYAG SAFICPEYRH
     LMKGVEKADS FNFNPHKWLL VNFDCSAMWL KEPRWIVDAF NVDPLYLKHD QQGSAP
//
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