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Database: UniProt/TrEMBL
Entry: B1IMT0_CLOBK
LinkDB: B1IMT0_CLOBK
Original site: B1IMT0_CLOBK 
ID   B1IMT0_CLOBK            Unreviewed;       467 AA.
AC   B1IMT0;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   20-DEC-2017, entry version 63.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=CLD_2710 {ECO:0000313|EMBL:ACA46668.1};
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA46668.1, ECO:0000313|Proteomes:UP000008541};
RN   [1] {ECO:0000313|EMBL:ACA46668.1, ECO:0000313|Proteomes:UP000008541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
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; CP000939; ACA46668.1; -; Genomic_DNA.
DR   RefSeq; WP_015958127.1; NC_010516.1.
DR   EnsemblBacteria; ACA46668; ACA46668; CLD_2710.
DR   KEGG; cbb:CLD_2710; -.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000008541; 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   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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:UP000008541};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:ACA46668.1};
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;  53706 MW;  64EAA183BB81E40C CRC64;
     MLYSSKNKQS NDTYATPIFG ITKDKYSIPK YKINENSIAP NIAYRMIKDE LMNEGNARLN
     LATFCQTYME DKATKLMAET LQKNAIDKSE YPQTAEIENR CVNIISDLWN VPKDMNFLGT
     STVGSSEACM LGGMSMKFRW RDQAKKLGID INKKKPNLVI SSGYQVCWEK FCVYWDIEMR
     TVPMDEDNLS LNMDKILDYV DEYTIGIIGI LGITYTGKFD DIKALDDAIE KYNSNHDIKV
     YIHVDAASGG FFTPFINPEI LWDFRLKNVV SINASGHKYG LVYPGIGWIL WKDQEYLPKD
     LIFEVSYLGG KMPTLAINFS RSGSQIIGQY YNFLRFGFEG YKKIHERTKE VAMYISKELE
     ATGLFSIYND GSNLPIVCYR LKEQSKVKWN LYDLSDRLAM KGWQIPAYPL PENLNHIIIQ
     RIVCRSDLGY NLAELLIKDF KTAINDLNNA HILFHEEENQ GIYGFTH
//
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