ID K3Y6R7_SETIT Unreviewed; 503 AA.
AC K3Y6R7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=101777099 {ECO:0000313|EnsemblPlants:KQK97466};
GN ORFNames=SETIT_7G115400v2 {ECO:0000313|EMBL:RCV33842.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK97466, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EMBL:RCV33842.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK97466,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV33842.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV33842.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV33842.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK97466}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK97466};
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; AGNK02004365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003534; RCV33842.1; -; Genomic_DNA.
DR RefSeq; XP_004975763.1; XM_004975706.1.
DR AlphaFoldDB; K3Y6R7; -.
DR STRING; 4555.K3Y6R7; -.
DR EnsemblPlants; KQK97466; KQK97466; SETIT_009908mg.
DR GeneID; 101777099; -.
DR Gramene; KQK97466; KQK97466; SETIT_009908mg.
DR KEGG; sita:101777099; -.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_019582_2_2_1; -.
DR InParanoid; K3Y6R7; -.
DR OMA; PNIVMSA; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000004995; Chromosome VII.
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:SF13; 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:UP000004995}.
FT MOD_RES 279
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 503 AA; 56157 MW; 976A42A264F8702B CRC64;
MVLTHVQELD DAAAASAVVF ASRYVQEPLP RFELGKKSIS KDAAYQIIHD ELLLDSSPRL
NLASFVTTWM EPECDRLILE GINKNYADMD EYPVTTEIQN RCVNIIARLF NAPVGAGEKA
VGVGTVGSSE AIMLAGLAFK RRWQNRRKAA GKPYDKPNIV TGANVQVCWE KFARYFEVEL
KEVKLREGCY VMDPDEAVQM VDENTICVAA ILGSTLTGEF EDVKRLNNLL LAKNKRTGWD
TPIHVDAASG GFIAPFLYPE LEWDFRLPLV KSINVSGHKY GLVYAGVGWV IWRNKEDLPE
DLIFHINYLG ADQPTFTLNF SKGSSQIIAQ YYQFLRLGFE GYRNVMENCM ESARTLREGL
ERTGRFTIIS KDQGVPLVAF TFKGKDTSLA FRLSSELRRF GWIVPAYTMP ANLEHMAVLR
VVVREDFGRP LAERFLSHVR MALEELDDEA KGGPVPRMRV TIELGPAAKG SGEEATARVV
KRESVVAVQR SVSLAGGKTK GVC
//
