ID   Q8T8A7_CIOIN            Unreviewed;       531 AA.
AC   Q8T8A7; A0A1W2VNG7;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   SubName: Full=Glutamic acid decarboxylase {ECO:0000313|EMBL:BAB88854.1};
GN   Name=Ci-GAD {ECO:0000313|EMBL:BAB88854.1};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|EMBL:BAB88854.1};
RN   [1] {ECO:0000313|EMBL:BAB88854.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20141424; DOI=10.2108/zsj.27.191;
RA   Takamura K., Minamida N., Okabe S.;
RT   "Neural map of the larval central nervous system in the ascidian Ciona
RT   intestinalis.";
RL   Zool. Sci. 27:191-203(2010).
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}.
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DR   EMBL; AB072597; BAB88854.1; -; mRNA.
DR   RefSeq; NP_001027785.1; NM_001032613.1.
DR   AlphaFoldDB; Q8T8A7; -.
DR   SMR; Q8T8A7; -.
DR   GeneID; 448951; -.
DR   KEGG; cin:448951; -.
DR   CTD; 448951; -.
DR   OrthoDB; 888358at2759; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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; PTHR45677:SF10; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
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         341
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   531 AA;  60719 MW;  AFD16187EDFACC6B CRC64;
     MQKQSAWRFR SSSVGLIKVE PNNDDYSMNN GDFENSSSAD LLPFGKSDEK TQLFLKEIFE
     ILLKYISKSF DRKCKILDFH HPHQLLEGIE GFSLNINGEA ESLEQILVDC RDTLKYGVKT
     GHPRFFNQLS SGLDIVSLAA DWVTSTANTN MFTFEIAPVF ILMEDVIIKR MMKIIGWENI
     DGIFSPGGSI NNLYSVMLAR HKIMPDVKHS GLRGFPQLVM FQSKHAHYSN KRPAAILGIG
     LNNCIDIEVD ERGHMKPEDL ELKILQSKLD GKVPFYVTAT AGTTVRGAFD EIVKISEVCK
     KYKIWLHVDA AWGGAVMMSQ KHRHLVAGIE MSDSVTWNPH KMVGVVLQCS MLLTKHKRLL
     ESCNNMRADY LFQQDKHYDI TYDTGDKTIQ CGRHVDVFKL WLSWRAKGDK GFCHHVERCI
     ELARYLVRKI KKTPGFQLVF QEPEYSNVCF WYYPPSIRNI CDEVIKNEKL GKVAPIIKSR
     MMERGSIMIG YQPLGSKVNF FRCVISNCAV NYDDIDFMVG QIERLGHDID M
//