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Database: UniProt/TrEMBL
Entry: C1FPE4_CLOBJ
LinkDB: C1FPE4_CLOBJ
Original site: C1FPE4_CLOBJ 
ID   C1FPE4_CLOBJ            Unreviewed;       467 AA.
AC   C1FPE4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   20-JUN-2018, entry version 58.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=CLM_2134 {ECO:0000313|EMBL:ACO85906.1};
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO85906.1, ECO:0000313|Proteomes:UP000001374};
RN   [1] {ECO:0000313|EMBL:ACO85906.1, ECO:0000313|Proteomes:UP000001374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2 {ECO:0000313|Proteomes:UP000001374};
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G.,
RA   Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP001581; ACO85906.1; -; Genomic_DNA.
DR   RefSeq; WP_011986457.1; NC_012563.1.
DR   ProteinModelPortal; C1FPE4; -.
DR   EnsemblBacteria; ACO85906; ACO85906; CLM_2134.
DR   KEGG; cby:CLM_2134; -.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000001374; 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:UP000001374};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:ACO85906.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     278    278       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   467 AA;  53660 MW;  533231CB09C8E733 CRC64;
     MLYSSKNKQS NDTYATPIFG ITKDKYSIPK YKINENSIAP NIAYRMIKDE LMNEGNARLN
     LATFCQTYME DKATKLMAET LQKNAIDKSE YPQTAEIENR CVNIISDLWN VPKDMNFLGT
     STVGSSEACM LGGMSMKFRW RDQAKKLGID INKKKPNLVI SSGYQVCWEK FCVYWDIEMR
     TVPMDEDNLS LNIDKILDYV DEYTIGIIGI LGITYTGKFD DIKALDDAIE KYNSNHDIKV
     YIHVDAASGG FFTPFINPEI LWDFRLKNVV SINASGHKYG LVYPGIGWIL WKDQEYLPKD
     LIFEVSYLGG KMPTLAINFS RSGSQIIGQY YNFLRFGFEG YKKIHERTKE VAMYISKELE
     ATGLFSIYND GSNLPIVCYK LKEQSKVKWN LYDLSDRLAM KGWQIPAYPL PENLNHIIIQ
     RIVCRSDLGY NLAELLIKDF KTAINDLNNA HILFHEEENQ GIYGFTH
//
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