ID A0A3B6C7X4_WHEAT Unreviewed; 486 AA.
AC A0A3B6C7X4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CFC21_023927 {ECO:0000313|EMBL:KAF7009388.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS2B02G333700.2};
RN [1] {ECO:0000313|EMBL:KAF7009388.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7009388.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS2B02G333700.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS2B02G333700.2};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS2B02G333700.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7009388.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7009388.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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; CM022215; KAF7009388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6C7X4; -.
DR PaxDb; 4565-Traes_2BL_EB3642842-1; -.
DR EnsemblPlants; TraesCS2B02G333700.2; TraesCS2B02G333700.2; TraesCS2B02G333700.
DR Gramene; TraesCS2B02G333700.2; TraesCS2B02G333700.2; TraesCS2B02G333700.
DR Gramene; TraesCS2B03G0868100.2; TraesCS2B03G0868100.2.CDS; TraesCS2B03G0868100.
DR Gramene; TraesKAR2B01G0322080.1; cds.TraesKAR2B01G0322080.1; TraesKAR2B01G0322080.
DR Gramene; TraesRN2B0100894800.2; TraesRN2B0100894800.2; TraesRN2B0100894800.
DR OMA; CLENARI; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000019116; Chromosome 2B.
DR Proteomes; UP000815260; Chromosome 2B.
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:UP000019116}.
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 486 AA; 55100 MW; 80C1A1FE301712FB CRC64;
MALSRAQTSS GESLISSTFA SRYVRTALPR FRMPEQSIPK DAAYQIINDE LMLDGNPRLN
LASFVTTWME PECDKLIQDS VNKNYVDMDE YPVTTEFQNR CVNMIAHLFN APIGEDETAV
GVGTVGSSEA IMLAGLAFKR KWQNKMKAEG KPHDKPNIVT GANVQVCWEK FARYFEVELK
EVKLREGYYV MDPEKAVELV DENTICVAAI LGSTLNGEFE DVKMLNDLLV AKNAETGWDT
PIHVDAASGG FIAPFIYPEL EWDFRLPLVK SINVSGHKYG LVYAGVGWVI WRNKEDLPDE
LIFHINYLGA DQPTFTLNFS KGSSQIIAQY YQLIRLGFEG YKDIMQNCRD NATVLREGVE
KMGYFHLVSK DSGVPLVAFS LKDSSKYTVF EVVESLRRFG WIVPAYTMPA DAEHIAVMRV
VIREDFSRGL AERLITDLKK VMVEMDAHAK KHGHHEHVKK TAHQIEKEVT TYWRTFVARK
KHSLVC
//
