ID   DCE_PETHY               Reviewed;         500 AA.
AC   Q07346;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Glutamate decarboxylase;
DE            Short=GAD;
DE            EC=4.1.1.15;
GN   Name=GAD;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Petal;
RX   PubMed=8366104; DOI=10.1016/s0021-9258(19)36560-3;
RA   Baum G., Chen Y., Arazi T., Takatsuji H., Fromm H.;
RT   "A plant glutamate decarboxylase containing a calmodulin binding domain.
RT   Cloning, sequence, and functional analysis.";
RL   J. Biol. Chem. 268:19610-19617(1993).
RN   [2]
RP   STRUCTURE BY NMR OF 470-495 IN COMPLEX WITH CALMODULIN, AND DIMERIZATION.
RX   PubMed=12684008; DOI=10.1016/s0022-2836(03)00271-7;
RA   Yap K.L., Yuan T., Mal T.K., Vogel H.J., Ikura M.;
RT   "Structural basis for simultaneous binding of two carboxy-terminal peptides
RT   of plant glutamate decarboxylase to calmodulin.";
RL   J. Mol. Biol. 328:193-204(2003).
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.
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12684008}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; L16797; AAA33709.1; -; mRNA.
DR   EMBL; L16977; AAA33710.1; -; mRNA.
DR   PIR; A48767; A48767.
DR   PDB; 1NWD; NMR; -; B/C=470-495.
DR   PDBsum; 1NWD; -.
DR   AlphaFoldDB; Q07346; -.
DR   BMRB; Q07346; -.
DR   SASBDB; Q07346; -.
DR   SMR; Q07346; -.
DR   EvolutionaryTrace; Q07346; -.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
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   IDEAL; IID50189; -.
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:SF41; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calmodulin-binding; Decarboxylase; Lyase;
KW   Pyridoxal phosphate.
FT   CHAIN           1..500
FT                   /note="Glutamate decarboxylase"
FT                   /id="PRO_0000146976"
FT   REGION          469..500
FT                   /note="Calmodulin-binding"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           474..492
FT                   /evidence="ECO:0007829|PDB:1NWD"
SQ   SEQUENCE   500 AA;  56726 MW;  72A043CB885AE10D CRC64;
     MVLSKTVSQS DVSIHSTFAS RYVRTSLPRF KMPDNSIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLMMDSI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLEDGETAVG
     VGTVGSSEAI MLAGLAFKRK WQNKMKAQGK PCDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLSEGYYVM DPEKAVEMVD ENTICVAAIL GSTLNGEFED VKRLNDLLVE KNKETGWDTP
     IHVDAASGGF IAPFIYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVVW RNKDDLPDEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGYEGY KNVMENCQEN ASVLREGLEK
     TGRFNIISKE IGVPLVAFSL KDNRQHNEFE ISETLRRFGW IVPAYTMPPN AQHITVLRVV
     IREDFSRTLA ERLVRDIEKV LHELDTLPAR VNAKLAVAEE QAAANGSEVH KKTDSEVQLE
     MITAWKKFVE EKKKKTNRVC
//