ID A0A0Q3KE10_BRADI Unreviewed; 508 AA.
AC A0A0Q3KE10;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=100832185 {ECO:0000313|EnsemblPlants:KQK22684};
GN ORFNames=BRADI_1g68807v3 {ECO:0000313|EMBL:KQK22684.1};
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:KQK22684.1};
RN [1] {ECO:0000313|EMBL:KQK22684.1, ECO:0000313|EnsemblPlants:KQK22684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK22684.1,
RC ECO:0000313|EnsemblPlants:KQK22684};
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:KQK22684.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK22684.1};
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:KQK22684}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK22684};
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; CM000880; KQK22684.1; -; Genomic_DNA.
DR EMBL; CM000880; PNT77787.1; -; Genomic_DNA.
DR RefSeq; XP_003558409.1; XM_003558361.2.
DR AlphaFoldDB; A0A0Q3KE10; -.
DR STRING; 15368.A0A0Q3KE10; -.
DR EnsemblPlants; KQK22684; KQK22684; BRADI_1g68807v3.
DR EnsemblPlants; PNT77787; PNT77787; BRADI_1g68807v3.
DR GeneID; 100832185; -.
DR Gramene; KQK22684; KQK22684; BRADI_1g68807v3.
DR Gramene; PNT77787; PNT77787; BRADI_1g68807v3.
DR KEGG; bdi:100832185; -.
DR InParanoid; A0A0Q3KE10; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000008810; Chromosome 1.
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:SF35; 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 508 AA; 57209 MW; 1F9A17906C9E422D CRC64;
MVLSKAVSDT DMSVHSTFAS RYVRSSLPRY RMPENSIPKE AAYQIINDEL MLDGNPRLNL
ASFVTTWMEP ECDKLIMASI NKNYVDMDEY PVTTELQNRC VNMIAHLFHA PLGESETAVG
VGTVGSSEAI MLAGLAFKRR WQNKRKAEGK PFDKPNIITG ANVQVCWEKF ARYFEVELKE
VKLREGYYVM DPDQAVEMVD ENTICVAAIL GSTLNGEFED VKRINDLLDK KNKETGWDTP
IHVDAASGGF IAPFLYPELE WDFRLPWVKS INVSGHKYGL VYAGIGWCIW RNAEDLPDEL
IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRHGFEGY RNIMENCQEN AMVLKEGLEK
TGRFNIVSKD EGVPLVAFSL KDHSRHDEFE ISDMLRRFGW IVPAYTMPAD AQHVTVLRVV
IREEFSRTLA ERLVLDIDKV MYQLDALPSN KLTPPAAAAA ALLPAATLVE KDVVVENGVA
KKSELEMQKS VTEALKKLAL ANKTNGVC
//
