ID   F8G9T7_FRAST            Unreviewed;       371 AA.
AC   F8G9T7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
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   OrderedLocusNames=F7308_0504 {ECO:0000313|EMBL:AEI35432.1};
OS   Francisella salina.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=573569 {ECO:0000313|EMBL:AEI35432.1, ECO:0000313|Proteomes:UP000000490};
RN   [1] {ECO:0000313|Proteomes:UP000000490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX07-7308 {ECO:0000313|Proteomes:UP000000490};
RA   Kuske C.R., Challacombe J.F., Siddaramappa S., Petersen J.M.;
RT   "The complete genome of Francisella sp. TX077308.";
RL   Submitted (MAY-2011) 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|ARBA:ARBA00000018,
CC         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; CP002872; AEI35432.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8G9T7; -.
DR   STRING; 573569.F7308_0504; -.
DR   KEGG; frt:F7308_0504; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_6; -.
DR   Proteomes; UP000000490; Chromosome.
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   Gene3D; 3.90.1150.160; -; 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:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT   COILED          340..367
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         189
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   371 AA;  42127 MW;  49F801913F15B317 CRC64;
     MVTQSKIWQH FVKLKWMILS TNLWNSSAEN AIGCSTTGSS EAAMLGGMAM KWRWRDKMKA
     QGKDYSKPNL VTGPVQVCWH KFARYWDIEL REIPMSKESL IMTPETTLEY CDENTIGVVP
     TFGVTFTGQY EPVETICEAL DEFEKETGID IPVHVDAASG GFLAPFIEPK LRWDFRLPRV
     KSINSSGHKF GLSPLGVGWV VWADKKYLPQ DLIFNVNYLG GDMPTFALNF SRPGGQIVAQ
     YYNFVKLGFE GYKNIHKLSY DVAKYISKEI KNMGIFDIIH AGKGGIPAVS WSLKASKSYD
     LFDISEKIRA KGWQIAAYSM PKHRENLVVM RVLVRRGFSF DLAELMIRDL KDVVDSLENK
     SKDIERSSFS H
//