ID Q8LKR4_TOBAC Unreviewed; 496 AA.
AC Q8LKR4;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|EMBL:AAM48129.1};
RN [1] {ECO:0000313|EMBL:AAM48129.1}
RP NUCLEOTIDE SEQUENCE.
RX DOI=10.1023/A:1023483106582;
RA McLean M.D., Yevtushenko D., Deschene A., Van Cauwenberghe O.R.,
RA Makhmoudova A., Potter J.W., Bown A.W., Shelp B.J.;
RT "Overexpression of glutamate decarboxylase in transgenic tobacco plants
RT confers resistance to the northern root-knot nematode.";
RL Mol. Breed. 11:277-285(2003).
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 Evidence={ECO:0000256|RuleBase:RU361171};
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|RuleBase:RU000382}.
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DR EMBL; AF506366; AAM48129.1; -; mRNA.
DR RefSeq; NP_001312769.1; NM_001325840.1.
DR AlphaFoldDB; Q8LKR4; -.
DR GeneID; 107809522; -.
DR KEGG; nta:107809522; -.
DR OrthoDB; 2783360at2759; -.
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 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 2: Evidence at transcript level;
KW Decarboxylase {ECO:0000256|RuleBase:RU361171};
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 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 496 AA; 55966 MW; 4771CF71BC478349 CRC64;
MVLSKTASES DVSIHSTFAS RYVRTSLPRF KMPENSIPKE AAYQIINDEL MLDGNPRLNL
ASFVTTWMEP ECNTLMMDSI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLGDGETAVG
VGTVGSSEAI MLAGLAFKRK WQNKMKAQGK PFDKPNIVTG ANVQVCWEKF ARYFEVELKE
VKLSDGYYVM DPEKAVEMVD ENTICVAAIL GSTLNGEFED VKRLNDLLIE KNKETGWDTP
IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWAIW RNKEDLPDEL
IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGFEGY KNVMENCQEN ARVLREGIEK
SGRFNIISKE IGVPLVAFSL KDNSQHNEFE ISETLRRFGW IVPAYTMPPN AQHVTVLRVV
IREDFSRTLA ERLVIDIEKV LHELDTLPAR VNAKLAVAEA NGSGVHKKTD REVQLEITTA
WKKFVADKKK KTNGVC
//
