ID Q7Z0K5_9MUSC Unreviewed; 281 AA.
AC Q7Z0K5;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 69.
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:AAM80945.1};
OS Drosophila arawakana kittensis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=201951 {ECO:0000313|EMBL:AAM80945.1};
RN [1] {ECO:0000313|EMBL:AAM80945.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wildcaught Wash Ghut 4 {ECO:0000313|EMBL:AAM80945.1};
RA Wilder J.A., Dyreson E., Spangler M.L., Sainz A.H., Hollocher H.;
RT "Molecular Footprints of Natural Selection on Pigmentation Genes in the
RT Drosophila dunni Subgroup.";
RL Submitted (JUN-2002) 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|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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY126887; AAM80945.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7Z0K5; -.
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 3: Inferred from homology;
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 179
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAM80945.1"
FT NON_TER 281
FT /evidence="ECO:0000313|EMBL:AAM80945.1"
SQ SEQUENCE 281 AA; 31262 MW; EB022643CE604849 CRC64;
MLDLPAEFLA CSGGKGGGVI QGTASESTLV ALLGAKAKKL QEVKAEHPEW DDHTIIGKLV
GYTSAQSHSS VERAGLLGGI KLRSVPADEH NRLRGDALEK AIEKDLAEGL IPFYAVVTLG
TTNSCAFDRL DECGPVANKH KVWVHVDAAY AGSTFICPEY RHHMKGIETA DSFNFNPHKW
MLVNFDCSAM WLKDPSWVVN AFNVDPLYLK HDMQGSAPDY RHWQIPLGRR FRALKLWFVL
RLYGVENLQA HIRRHCGFAQ QFADLCVADE RFELAAEVNM G
//