DCE_PETHY
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 25-MAY-2022, entry version 96.
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 Gene3D; 3.40.640.10; -; 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 PANTHER; PTHR43321; PTHR43321; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01788; Glu-decarb-GAD; 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