ID A0A3B6I428_WHEAT Unreviewed; 454 AA.
AC A0A3B6I428;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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_054462 {ECO:0000313|EMBL:KAF7045350.1};
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:TraesCS4A02G369200.1};
RN [1] {ECO:0000313|EMBL:KAF7045350.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7045350.1};
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:TraesCS4A02G369200.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4A02G369200.1};
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:TraesCS4A02G369200.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7045350.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7045350.1};
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; CM022220; KAF7045350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6I428; -.
DR SMR; A0A3B6I428; -.
DR STRING; 4565.A0A3B6I428; -.
DR EnsemblPlants; TraesCS4A02G369200.1; TraesCS4A02G369200.1; TraesCS4A02G369200.
DR Gramene; TraesCS4A02G369200.1; TraesCS4A02G369200.1; TraesCS4A02G369200.
DR Gramene; TraesCS4A03G0908800.1; TraesCS4A03G0908800.1.CDS; TraesCS4A03G0908800.
DR Gramene; TraesROB_scaffold_007440_01G000900.1; TraesROB_scaffold_007440_01G000900.1; TraesROB_scaffold_007440_01G000900.
DR OMA; LHIDTVM; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000019116; Chromosome 4A.
DR Proteomes; UP000815260; Chromosome 4A.
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:UP000019116}.
FT MOD_RES 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 454 AA; 51759 MW; 6DFCB0046EC7EEF8 CRC64;
MVLSRAVSDT DVSVHSTFAS RYVRSSLPRY HMPEKSIPKE AAYQIINDEL MLDGNPRLNL
ASFVTTWMEP ECDKLVMASM NKNYVDMDEY PVTTEFQNRC VNMIAHLFHA PLGESETAVG
VGTVGSSEAI MLAGLAFKRK WQNKRRAEGK PFDKPNIVTG ANVQVCWEKF ARYFEVELKE
VKLREGYYVM DPEQAVEMVD ENTICVAAIL GSTLNGEFED VKRINDLLEE KNKETGWETA
IHVDAASGGF IAPFLYPELE WDFRLPWVKS INVSGHKYGL VYPGIGWCVW RTKDDLPDDL
VFHINYLGTD QPTFTLNFSK GSSQVIAQYY QFIRQGFEGY RNIMENCQEN AMVVKEGLER
TGRFNIVSKD QGVPLVAFSL KDHTRHDEFE VSDMLRRFGW IVPAYTMPAD AQHVTVLRVV
IREEFSRTLA ERLVLHIDTV MNQLDALPSN SVCQ
//
