ID   DCE_SOLLC               Reviewed;         502 AA.
AC   P54767;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=Glutamate decarboxylase;
DE            Short=GAD;
DE            EC=4.1.1.15;
DE   AltName: Full=ERT D1;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ailsa Craig; TISSUE=Pericarp;
RX   PubMed=7766895; DOI=10.1007/bf00020887;
RA   Gallego P.P., Whotton L., Picton S., Grierson D., Gray J.E.;
RT   "A role for glutamate decarboxylase during tomato ripening: the
RT   characterisation of a cDNA encoding a putative glutamate decarboxylase with
RT   a calmodulin-binding site.";
RL   Plant Mol. Biol. 27:1143-1151(1995).
CC   -!- FUNCTION: Catalyzes the production of GABA. The calmodulin-binding is
CC       calcium-dependent and it is proposed that this may, directly or
CC       indirectly, form a calcium regulated control of GABA biosynthesis (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; X80840; CAA56812.1; -; mRNA.
DR   PIR; S56177; S56177.
DR   AlphaFoldDB; P54767; -.
DR   SMR; P54767; -.
DR   STRING; 4081.P54767; -.
DR   PaxDb; 4081-Solyc03g098240-2-1; -.
DR   ProMEX; P54767; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   InParanoid; P54767; -.
DR   BioCyc; MetaCyc:MONOMER-15560; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P54767; baseline.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF37; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Decarboxylase; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..502
FT                   /note="Glutamate decarboxylase"
FT                   /id="PRO_0000146975"
FT   REGION          471..502
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  56785 MW;  1C5F9BD0084272A6 CRC64;
     MVLTTTSIRD SEESLHCTFA SRYVQEPLPK FKMPKKSMPK EAAYQIVNDE LMLDGNPRLN
     LASFVSTWME PECDKLIMSS INKNYVDMDE YPVTTELQNR CVNMLAHLFH APVGDDETAV
     GVGTVGSSEA IMLAGLAFKR KWQSKRKAEG KPFDKPNIVT GANVQVCWEK FARYFEVELK
     EVKLKEGYYV MDPAKAVEIV DENTICVAAI LGSTLTGEFE DVKLLNELLT KKNKETGWET
     PIHVDAASGG FIAPFLWPDL EWDFRLPLVK SINVSGHKYG LVYAGVGWVI WRSKEDLPDE
     LVFHINYLGS DQPTFTLNFS KGSYQIIAQY YQLIRLGFEG YKNVMKNCLS NAKVLTEGIT
     KMGRFDIVSK DVGVPVVAFS LRDSSKYTVF EVSEHLRRFG WIVPAYTMPP DAEHIAVLRV
     VIREDFSHSL AERLVSDIEK ILSELDTQPP RLPTKAVRVT AEEVRDDKGD GLHHFHMDTV
     ETQKDIIKHW RKIAGKKTSG VC
//