ID   B1KTZ5_CLOBM            Unreviewed;       467 AA.
AC   B1KTZ5;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
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=CLK_1372 {ECO:0000313|EMBL:ACA53668.1};
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA53668.1, ECO:0000313|Proteomes:UP000000722};
RN   [1] {ECO:0000313|EMBL:ACA53668.1, ECO:0000313|Proteomes:UP000000722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000962; ACA53668.1; -; Genomic_DNA.
DR   RefSeq; WP_012341867.1; NC_010520.1.
DR   AlphaFoldDB; B1KTZ5; -.
DR   KEGG; cbl:CLK_1372; -.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   Proteomes; UP000000722; Chromosome.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
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:SF3; 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}.
FT   MOD_RES         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   467 AA;  53664 MW;  4BC052808BAA1A06 CRC64;
     MLYSSKNKQS NDTYATPIFG ITKDKYSIPK YKINENSIAP NIAYRMIKDE LMNEGNARLN
     LATFCQTYME DKATKLMAET LQKNAIDKSE YPQTAEIENR CVNIISDLWN VPKDMNFLGT
     STVGSSEACM LGGMSMKFRW RDQAKKLGID INKKKPNLVI SSGYQVCWEK FCVYWDIEMR
     TVPMDEDNLS LNIDKILDYV DEYTIGIIGI LGITYTGKFD DIKALDDAIE KYNSNHDMKV
     YIHVDAASGG FFTPFINPEI LWDFRLKNVV SINASGHKYG LVYPGIGWIL WKDQEYLPKD
     LIFEVSYLGG KMPTLAINFS RSGSQIIGQY YNFLRFGFEG YKKIHERTKE VAMYISKELE
     ATGLFSIYND GSNLPIVCYK LKEQSNVKWN LYDLSDRLAM KGWQIPAYPL PENLNHIIIQ
     RIVCRSDLGY NLAELLIKDF KTAINDLNNA HILFHEEENQ GIYGFTH
//