ID   T1DQ67_ANOAQ            Unreviewed;       498 AA.
AC   T1DQ67;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
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;
OS   Anopheles aquasalis (Malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=42839 {ECO:0000313|EMBL:JAB00246.1};
RN   [1] {ECO:0000313|EMBL:JAB00246.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole body {ECO:0000313|EMBL:JAB00246.1};
RG   Brazilian Malaria Network (MCT/CNPq/MS/SCTIE/DECIT/PRONEX 555648/2009-5) and Research Network on Bioactive Molecules from Arthropod Vectors (NAP-MOBIARVE;
RG   University of Sao Paulo);
RA   Marinotti O., Ribeiro J.M.C., Costa-da-Silva A.L., Silva M.C.P.,
RA   Lopes A.R., Barros M.S., Sa-Nunes A., Konjin B.B., Carvalho E., Suesdek L.,
RA   Silva-Neto M.A.C., Capurro M.L.;
RT   "Transcriptome sequencing and developmental regulation of gene expression
RT   in Anopheles aquasalis.";
RL   Submitted (JUL-2013) 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   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; GAMD01001345; JAB00246.1; -; mRNA.
DR   AlphaFoldDB; T1DQ67; -.
DR   VEuPathDB; VectorBase:AAQUA_002394; -.
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   MOD_RES         322
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB00246.1"
SQ   SEQUENCE   498 AA;  56400 MW;  4280BF514BB1E91F CRC64;
     TLNRNNSFKM PVPLEKRTEM QAPEFKDFAK EMVDYISNYL ENIRDRRVLP TVQPGYLRPL
     IPDEAPQQPD KWEDVMADIE RVIMPGVTHW HSPKFHAYFP TANSYPAIVA DMLSGAIACI
     GFTWIASPAC TELEVVMLDW LGKMLDLPKE FLACSGGQGG GVIQGTASEA TLVGLLGAKA
     KAMKRVKEEH PDWDDNTIVS KLVGYTSIQS HSSVERAGLL GGVKLRSLAS DADLKLRGET
     LERAIKEDLE AGLIPFYVVA TLGTTNTCAF DRLDEIGPIG NKYNVWVHVD AAYAGSAFIC
     PEYRYLMKGI ETADSFNFNP HKWMLVNFDC SAMWLKEPYW IVNAFNVDPL YLKHDMQGSA
     PDYRHWQIPL GRRFRALKLW FVLRLYGIDN LQAHIRRHCA FAKQFETLCR ADERFEIFGE
     VQMGLACFKL KGSNELNEQL LRRINGRGNI HLVPSKVNDV YFLRMAVCSR FTESPDIDYS
     WKEVAASADE VLAEQQKK
//