ID B3TGG1_PAPGL Unreviewed; 124 AA.
AC B3TGG1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-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:ABX57257.1};
OS Papilio glaucus (Eastern tiger swallowtail butterfly) (Pterourus glaucus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio; Pterourus.
OX NCBI_TaxID=45779 {ECO:0000313|EMBL:ABX57257.1};
RN [1] {ECO:0000313|EMBL:ABX57257.1}
RP NUCLEOTIDE SEQUENCE.
RA Wahlberg N., Wheat C.W.;
RT "Genomic Outposts Serve the Phylogenomic Pioneers: Designing Novel Nuclear
RT Markers for Genomic DNA Extractions of Lepidoptera.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC 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; EU141433; ABX57257.1; -; Genomic_DNA.
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 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000382}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABX57257.1"
FT NON_TER 124
FT /evidence="ECO:0000313|EMBL:ABX57257.1"
SQ SEQUENCE 124 AA; 14911 MW; 566E64099ECFBA77 CRC64;
GSAFICPEYR YLMKGXXXXX SFNFNPHKWM NVNFDCSAMW LKQPRWIVDA FNVDPLYLKH
DQQGSAPDYR HWQIPLGRRF RALKLWFVLR LYGVENLQKH IRKHIALAHL FEKLCTSDER
FEIV
//