ID Q9Y0P0_9NEOP Unreviewed; 217 AA.
AC Q9Y0P0;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-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:AAD37659.1};
OS Acronicta sp. near modica Mitter 166.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Acronictinae; Acronicta.
OX NCBI_TaxID=62934 {ECO:0000313|EMBL:AAD37659.1};
RN [1] {ECO:0000313|EMBL:AAD37659.1}
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:AAD37659.1}
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; AF151576; AAD37659.1; -; mRNA.
DR AlphaFoldDB; Q9Y0P0; -.
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 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:AAD37659.1"
FT NON_TER 217
FT /evidence="ECO:0000313|EMBL:AAD37659.1"
SQ SEQUENCE 217 AA; 24164 MW; 8D4986808CAD5D7E CRC64;
LGLPESFLAR SNGEAGGVIQ GTASEATLVA LLGAKTRMIL RVKEKHPEWT DNEIISKLVG
YCNKQAHSSV ERAGLLGGVK LRTLQPDEKR RLRGDVLQDA IEEDIRNGLI PFYVVATLGT
TSSCSFDVLD EIGDVCRSHD LWLHVDAAYA GSAFICPEYR YLMQGVEKAD SFNFNPHKWL
LVNFDCSAMW LKEPRWIVDA FNVDPLYLKH DQQGSAP
//
