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Database: UniProt/TrEMBL
Entry: B1KTZ5_CLOBM
LinkDB: B1KTZ5_CLOBM
Original site: B1KTZ5_CLOBM 
ID   B1KTZ5_CLOBM            Unreviewed;       467 AA.
AC   B1KTZ5;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   25-APR-2018, entry version 63.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=CLK_1372 {ECO:0000313|EMBL:ACA53668.1};
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; 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-
RT   A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         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   EnsemblBacteria; ACA53668; ACA53668; CLK_1372.
DR   KEGG; cbl:CLK_1372; -.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; CBOT498214:GH05-2022-MONOMER; -.
DR   Proteomes; UP000000722; 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; 3.40.640.10; -; 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   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000722};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:ACA53668.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     278    278       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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