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Database: UniProt
Entry: G3E6N2_9MUSC
LinkDB: G3E6N2_9MUSC
Original site: G3E6N2_9MUSC 
ID   G3E6N2_9MUSC            Unreviewed;       188 AA.
AC   G3E6N2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 31.
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:AEM77207.1};
OS   Drosophila birchii.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46829 {ECO:0000313|EMBL:AEM77207.1};
RN   [1] {ECO:0000313|EMBL:AEM77207.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21985965; DOI=10.1016/j.ympev.2011.09.018;
RA   Yang Y., Hou Z.C., Qian Y.H., Kang H., Zeng Q.T.;
RT   "Increasing the data size to accurately reconstruct the phylogenetic
RT   relationships between nine subgroups of the Drosophila melanogaster species
RT   group (Drosophilidae, Diptera).";
RL   Mol. Phylogenet. Evol. 62:214-223(2012).
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|RuleBase:RU000382}.
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DR   EMBL; HQ631620; AEM77207.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3E6N2; -.
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   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.
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:AEM77207.1"
FT   NON_TER         188
FT                   /evidence="ECO:0000313|EMBL:AEM77207.1"
SQ   SEQUENCE   188 AA;  20053 MW;  6CF06B40D7F8BD89 CRC64;
     AIACIGFTWI ASPACTELEV VMMDWLGKML DLPAEFLACS GGKGGGVIQG TASESTLVAL
     LGAKAKKVQE VKAQHPEWDD HTIVGKLVGY CSDQAHSSVE RAGLLGGVRL QSVPSENHRM
     RGDALEKAIE QDLAEGLIPF YAVVTLGTTN SCAFDYLDEC GPVGNKHNVW IHVDAAYAGS
     AFICPEYR
//
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