ID A0A0E0DEV4_9ORYZ Unreviewed; 484 AA.
AC A0A0E0DEV4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
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};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI04G12720.3};
RN [1] {ECO:0000313|EnsemblPlants:OMERI04G12720.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI04G12720.3};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI04G12720.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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 AlphaFoldDB; A0A0E0DEV4; -.
DR SMR; A0A0E0DEV4; -.
DR STRING; 40149.A0A0E0DEV4; -.
DR EnsemblPlants; OMERI04G12720.1; OMERI04G12720.1; OMERI04G12720.
DR EnsemblPlants; OMERI04G12720.3; OMERI04G12720.3; OMERI04G12720.
DR Gramene; OMERI04G12720.1; OMERI04G12720.1; OMERI04G12720.
DR Gramene; OMERI04G12720.3; OMERI04G12720.3; OMERI04G12720.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_019582_2_2_1; -.
DR Proteomes; UP000008021; Chromosome 4.
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: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:UP000008021}.
FT MOD_RES 276
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 484 AA; 54425 MW; 2A9ADCAA22D55CC7 CRC64;
MALSTAQTGE SMHSSTFASR YVRTALPRFR MPEKSIPKDA AYQIINDELM LDGNPRLNLA
SFVTTWMEPE CDKLMMAAIN KNYVDMDEYP VTTELQNRCV NMIAHLFNAP IGDDETAVGV
GTVGSSEAIM LAGLAFKRKW QNRMKAEGKP HDKPNIVTGA NVQVCWEKFA RYFEVELKEV
KLTQGYYVMN PEKAVEMVDE NTICVAAILG STLNGEFEDV KMLNDLLTAK NAETGWNTPI
HVDAASGGFI APFIYPELEW DFRLPLVKSI NVSGHKYGLV YAGVGWVIWR NKEDLPDELI
FHINYLGADQ PTFTLNFSKG SNQIIAQYYQ LIRLGFEGYK DIMQNCRDNA TVLREGIEKT
GHFDVVSKDS GVPLVAFSLK DSSRYTVFEV AESLRRFGWI VPAYTMPADA EHVAVMRVVI
REDFSRGLAE RLITDLTKTV ADMDAHAVKK AAAEPAKKTV REIEKEVTTY WRSFVARKKS
SLVC
//
