ID   D7LWZ5_ARALL            Unreviewed;       502 AA.
AC   D7LWZ5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
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_488599 {ECO:0000313|EMBL:EFH48020.1};
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|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=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; GL348718; EFH48020.1; -; Genomic_DNA.
DR   RefSeq; XP_002871761.1; XM_002871715.1.
DR   AlphaFoldDB; D7LWZ5; -.
DR   STRING; 81972.D7LWZ5; -.
DR   EnsemblPlants; fgenesh2_kg.6__1733__AT5G17330.1; fgenesh2_kg.6__1733__AT5G17330.1; fgenesh2_kg.6__1733__AT5G17330.1.
DR   GeneID; 9309890; -.
DR   Gramene; fgenesh2_kg.6__1733__AT5G17330.1; fgenesh2_kg.6__1733__AT5G17330.1; fgenesh2_kg.6__1733__AT5G17330.1.
DR   KEGG; aly:9309890; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005516; F:calmodulin binding; IEA:EnsemblPlants.
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   3: Inferred from homology;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   502 AA;  56933 MW;  48C1FB7E1CC1742B CRC64;
     MVLSHAASES DVSVHSTFAS RYVRTSLPRF KMPENSIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLIMSSI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLGETETAVG
     VGTVGSSEAI MLAGLAFKRK WQNKRKAEGK PVDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLSEGYYVM DPQKAVDMVD ENTICVAAIL GSTLNGEFED VKLLNDLLVE KNKETGWDTP
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RNKEDLPEEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGHEGY TNVMENCREN MIVLRKGLEK
     TERFNIVSKD EGVPLVAFSL KDNSSHTEFE ISDMLRRYGW IVPAYTMPPN AQHITVLRVV
     IREDFSRTLA ERLVIDIEKV MRELDELPSR VIHKISLGQE KSEANSDNVM VTVKKSDVEK
     QRDIIIGWKK FVADRKKTSG IC
//