ID   I1IY80_BRADI            Unreviewed;       488 AA.
AC   I1IY80;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-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=100831497 {ECO:0000313|EnsemblPlants:KQJ82853};
GN   ORFNames=BRADI_5g11600v3 {ECO:0000313|EMBL:KQJ82853.1};
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|EnsemblPlants:KQJ82853};
RN   [1] {ECO:0000313|EMBL:KQJ82853.1, ECO:0000313|EnsemblPlants:KQJ82853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ82853.1,
RC   ECO:0000313|EnsemblPlants:KQJ82853};
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:KQJ82853.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ82853.1};
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:KQJ82853}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ82853};
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; CM000884; KQJ82853.1; -; Genomic_DNA.
DR   RefSeq; XP_003579849.1; XM_003579801.3.
DR   AlphaFoldDB; I1IY80; -.
DR   STRING; 15368.I1IY80; -.
DR   EnsemblPlants; KQJ82853; KQJ82853; BRADI_5g11600v3.
DR   GeneID; 100831497; -.
DR   Gramene; KQJ82853; KQJ82853; BRADI_5g11600v3.
DR   KEGG; bdi:100831497; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; I1IY80; -.
DR   OMA; VGWVFWR; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000008810; Chromosome 5.
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:SF22; GLUTAMATE DECARBOXYLASE 5; 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         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   488 AA;  54995 MW;  7F2A8720C91974CA CRC64;
     MALSRAQTNH GESLISSTFA SRYVRAALPR FKIPEQSIPK EAAYQIINDE LMLDGNPRLN
     LASFVTTWME PECDKLIQNS INKNYVDMDE YPVTTELQNR CVNMIAHLFN APIGDDETAV
     GVGTVGSSEA IMLAGLAFKR KWQNKMKAAG KPFDKPNIVT GANVQVCWEK FARYFEVELK
     EVKLREGYYV MDPEKAVELV DENTICVAAI LGSTLNGEFE DVKMLNDLLV AKNAETGWDT
     PIHVDAASGG FIAPFIYPEL EWDFRLPLVK SINVSGHKYG LVYAGVGWVV WRTKDDLPDE
     LIFHINYLGA DQPTFTLNFS KGSSQIIAQY YQLIRLGFEG YKDIMQNCRD NATVLREGID
     KMGYFDIASK DSGVPLVAFS LKDSSRYTVF EVVESLRRFG WIVPAYTMPA DAEHIAVMRV
     VIREDFSRGL AERLITDLNK VMGEMDTHAK KHVAAEPPVA KKTVHEIEKE VATYWRRLVD
     RKKSSLVC
//