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Database: UniProt/TrEMBL
Entry: A0A0A7FVJ5_9CLOT
LinkDB: A0A0A7FVJ5_9CLOT
Original site: A0A0A7FVJ5_9CLOT 
ID   A0A0A7FVJ5_9CLOT        Unreviewed;       467 AA.
AC   A0A0A7FVJ5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   20-JUN-2018, entry version 23.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=U729_925 {ECO:0000313|EMBL:AIY83613.1};
OS   Clostridium baratii str. Sullivan.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY83613.1, ECO:0000313|Proteomes:UP000030635};
RN   [1] {ECO:0000313|EMBL:AIY83613.1, ECO:0000313|Proteomes:UP000030635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sullivan {ECO:0000313|EMBL:AIY83613.1};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H.,
RA   Foster J.T., Johnson S.L., Chertkov O., Teshima H., Gibbons H.S.,
RA   Johnsky L.A., Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
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; CP006905; AIY83613.1; -; Genomic_DNA.
DR   RefSeq; WP_039312061.1; NZ_CP006905.1.
DR   EnsemblBacteria; AIY83613; AIY83613; U729_925.
DR   GeneID; 31578181; -.
DR   KEGG; cbv:U729_925; -.
DR   KO; K01580; -.
DR   Proteomes; UP000030635; 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:UP000030635};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AIY83613.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030635}.
FT   MOD_RES     278    278       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   467 AA;  53315 MW;  4A18B87617E2CB21 CRC64;
     MLFTKENKIG NDTYKTPVFG ALEEDVDLPK YKLAKDPVEP RIAYRLVKDQ LMDEGNARLN
     LATFCQTYME DEATKLMSET LEKNAIDKSE YPQTTELENR CVNIIADLWH APENMNYLGT
     STVGSSEACM LGGMAMKFRW RNRAKALGMD VNNRKPNLVV SSGFQVCWEK FCVYWDIEMR
     LVPLDEEHMS LDVDKVLDYV DDYTIGVVGI LGITYTGKYD DIKKLDAVLE EYNKTAKISV
     PIHVDAASGG LFAPFIEPDL EWDFRLKNVV SISTSGHKYG LVYPGIGWVM WKDEEYLPKE
     LIFEVSYLGG QLPTMAINFS RSASQIIGQY YNFLRYGFEG YRRIHQRTKD VAMYLSKEIE
     NMGLFEIYND GENLPIVCFK LKDDANVNWT SYDLADRLAM KGWQVPAYPL PENLQDTTIQ
     RIVCRADLGH SMAEQLIADM KTGIEDLNKA TLLCHGKETK GKYGFTH
//
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