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
//