ID   Q94KK8_TOBAC            Unreviewed;       491 AA.
AC   Q94KK8;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 91.
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:AAK38667.1};
RN   [1] {ECO:0000313|EMBL:AAK38667.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12837817; DOI=10.1093/jxb/erg210;
RA   Yevtushenko D.P., McLean M.D., Peiris S., Van Cauwenberghe O.R.,
RA   Shelp B.J.;
RT   "Calcium/calmodulin activation of two divergent glutamate decarboxylases
RT   from tobacco.";
RL   J. Exp. Bot. 54:2001-2002(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; AF353615; AAK38667.1; -; mRNA.
DR   RefSeq; NP_001312970.1; NM_001326041.1.
DR   AlphaFoldDB; Q94KK8; -.
DR   GeneID; 107819266; -.
DR   KEGG; nta:107819266; -.
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:SF3; 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   491 AA;  55950 MW;  51CB78B3EF3F4E35 CRC64;
     MVLSKTSSES DVSVHSTFAS RYVRTSLPRF EMAENSIPKE AAFQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLMMDSI NKNYVDMDEY PVTTELQNRC VNMIARLFNA PLEEKETAVG
     VGTVGSSEAI MLAGLAFKRN WQNKRKAEGK PYNKPNIVTG ANVQVCWEKF ANYFEVELKE
     VKLREGYYVM DPVQAVEMVD ENTICVAAIL GSTLNGEFED VKLLNDLLIE KNKQTGWNTP
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RTKQDLPEEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGYEGY RNVMENCREN AIVLREGLEK
     TGRFNIVSKD EGVPLVAFSL KDNSRHNEFE VSETLRRFGW IVPAYTMPAD AQHVTVLRVV
     IREDFSRTLA ERLVLDIVKV LHELDTLPAR LSAKLEEVKL VKNGKKFELE VQREVTNYWK
     KFVLARKAPV C
//