ID   I1I7Q1_BRADI            Unreviewed;       499 AA.
AC   I1I7Q1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 65.
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   Name=100827187 {ECO:0000313|EnsemblPlants:KQJ98585};
GN   ORFNames=BRADI_3g37830v3 {ECO:0000313|EMBL:KQJ98585.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ98585.1};
RN   [1] {ECO:0000313|EMBL:KQJ98585.1, ECO:0000313|EnsemblPlants:KQJ98585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ98585.1,
RC   ECO:0000313|EnsemblPlants:KQJ98585};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQJ98585.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ98585.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQJ98585}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ98585};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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; CM000882; KQJ98585.1; -; Genomic_DNA.
DR   RefSeq; XP_003574600.1; XM_003574552.3.
DR   AlphaFoldDB; I1I7Q1; -.
DR   STRING; 15368.I1I7Q1; -.
DR   EnsemblPlants; KQJ98585; KQJ98585; BRADI_3g37830v3.
DR   GeneID; 100827187; -.
DR   Gramene; KQJ98585; KQJ98585; BRADI_3g37830v3.
DR   KEGG; bdi:100827187; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; I1I7Q1; -.
DR   OMA; KNIMQNC; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000008810; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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:SF37; 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:UP000008810}.
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   499 AA;  55820 MW;  A67E3FA81C171F07 CRC64;
     MVLSRAISSA GDSVACTFAS RYVREELPRY RMPEQSIPKE AAYQIITDEL MLDGNPRLNL
     ASFVTTWMEP ECAKLMMDSV NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PIKEDETAIG
     VSTVGSSEAI MLAGLAFKRK WQNKRKEQGK PCDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLTEGYYVM DPLKAVEMVD ENTICVAAIL GSTLTGEYED VKLLNDLLVE KNKETGWNVP
     IHVDAASGGF IAPFLQPELE WDFRLPLVKS INVSGHKYGL VYPGVGWVIW RSKDDLPDEL
     IFHINYLGTD QPTFTLNFSK GASQIIAQYY QLIRLGFEGY KHIMENCKGN AAILREGIEA
     TGRFKVLSKE DGVPLLAISL KDSTGFTVFD ISENLRRFGW IVPAYTMPAD AEHVAVLRVV
     IREDFSRSLA QRLIADINKV LRELDAHAVH AVKITTAVAT QASEGMDDGV VTKKSVLDTE
     KEFASACMDL LKNKKTGVC
//