ID   D7LPY5_ARALL            Unreviewed;       493 AA.
AC   D7LPY5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   02-SEP-2026, entry version 87.
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};
GN   ORFNames=ARALYDRAFT_484123 {ECO:0000313|EMBL:EFH53052.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|EMBL:EFH53052.1, ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + H(+) = 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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; GL348717; EFH53052.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7LPY5; -.
DR   STRING; 81972.D7LPY5; -.
DR   Gramene; fgenesh2_kg.5__115__AT2G02010.1; fgenesh2_kg.5__115__AT2G02010.1; fgenesh2_kg.5__115__AT2G02010.1.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   OrthoDB; 5152799at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:L-glutamate catabolic process; IEA:TreeGrafter.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   FunFam; 3.40.640.10:FF:000022; Glutamate decarboxylase; 1.
DR   FunFam; 3.90.1150.160:FF:000001; Glutamate decarboxylase; 1.
DR   FunFam; 4.10.280.50:FF:000002; Glutamate decarboxylase; 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:SF38; GLUTAMATE DECARBOXYLASE 3-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW   ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          33..381
FT                   /note="Pyridoxal phosphate-dependent decarboxylase major"
FT                   /evidence="ECO:0000259|Pfam:PF00282"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   493 AA;  55999 MW;  555875CF14796AAC CRC64;
     MVLSKTASES DVSIHSTFAS RYVRNSLPRF EMPENSIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLMMESI NKNYVDMDEY PVTTELQNRC VNMIARLFNA PLGDGEAAVG
     VGTVGSSEAI MLAGLAFKRQ WQNKRKAQGL PYDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VNLREDYYVM DPEKAVEMVD ENTICVAAIL GSTLTGEFED VKLLNDLLVE KNKQTGWDTP
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVVW RTKTDLPDEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGFEGY RNVMDNCREN MMVLRQGLEK
     TGRFNIVSKE NGVPLVAFSL KDSSRHNEFE VAETLRRFGW IVPAYTMPAD AQHVTVLRVV
     IREDFSRTLA ERLVADFEKV LHELDTLPAR IHAKMANGKV NGVKKTPEET QREVTAYWKK
     LLETKKTNKN TIC
//