ID O45216_CERCA Unreviewed; 431 AA.
AC O45216;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 90.
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};
GN Name=Ddc {ECO:0000313|EMBL:CAA69668.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:CAA69668.1};
RN [1] {ECO:0000313|EMBL:CAA69668.1}
RP NUCLEOTIDE SEQUENCE.
RA Mantzouridis T.D.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAA69668.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9434169; DOI=10.1016/S0378-1119(97)00527-1;
RA Mantzouridis T.D., Sideris D.C., Fragoulis E.G.;
RT "cDNA cloning of L-dopa decarboxylase from the eclosion stage of the insect
RT Ceratitis capitata. Evolutionary relationship to other species
RT decarboxylases.";
RL Gene 204:85-89(1997).
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; Y08388; CAA69668.1; -; mRNA.
DR AlphaFoldDB; O45216; -.
DR BRENDA; 4.1.1.28; 1254.
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 CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
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; IPR015422; PyrdxlP-dep_Trfase_small.
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 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 REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 308
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 431 AA; 47865 MW; B203C1A51A90E60D CRC64;
MSHIPISNTI PTKQTDGNGK ANISPDKLDP KVSRVLPEVK PGYLKPLIPD AAPEKPEKWQ
DVMQDIERVI MPGVTHWHSP KLHAYFPTAN SYPAIVADML SGAIACIGFT WIASPACTQL
EVVMMDWLGK MLELPAEFLA CSGGKGGGVI QGTASGSTLV ALLGAKAKKL KEVKELHPEW
DEHTILGKLA GYCSDQAHSS VERAGLLGGV KLGSVQSENH RMRGAALEKA IEQDVAEGRI
PFYAVVTLGT TNSCAFDYLD ECGPVGNKHN LWIHLDAAYA GSAFICMEYR HPMKGIEMAD
SFNFNPHKWM RVNFDCSAMW LKDPSWVVNA FNADPLYLYP KHDMQGSAPD YRHWQIPLGR
RFRALKLWFV LRLYGVENLQ AHIRRHCNFA KQFGDLCVAH SRFEPAAEIN MGLVCFRLTD
TLVVQEIIGR K
//
