GenomeNet

Database: UniProt/TrEMBL
Entry: M4KCQ4_LACPN
LinkDB: M4KCQ4_LACPN
Original site: M4KCQ4_LACPN 
ID   M4KCQ4_LACPN            Unreviewed;       469 AA.
AC   M4KCQ4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   25-APR-2018, entry version 29.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gadB {ECO:0000313|EMBL:AGE37597.1};
GN   ORFNames=zj316_0058 {ECO:0000313|EMBL:AGE37597.1};
OS   Lactobacillus plantarum ZJ316.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1284663 {ECO:0000313|EMBL:AGE37597.1, ECO:0000313|Proteomes:UP000011825};
RN   [1] {ECO:0000313|EMBL:AGE37597.1, ECO:0000313|Proteomes:UP000011825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZJ316 {ECO:0000313|EMBL:AGE37597.1};
RX   PubMed=23516215;
RA   Li X., Gu Q., Lou X., Zhang X., Song D., Shen L., Zhao Y.;
RT   "Complete genome sequence of the probiotic Lactobacillus plantarum
RT   strain ZJ316.";
RL   Genome Announc. 1:E0009413-E0009413(2013).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP004082; AGE37597.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGE37597; AGE37597; zj316_0058.
DR   KEGG; lpt:zj316_0058; -.
DR   PATRIC; fig|1284663.3.peg.57; -.
DR   KO; K01580; -.
DR   Proteomes; UP000011825; 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:UP000011825};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:AGE37597.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     280    280       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   469 AA;  53557 MW;  8A9670113958D735 CRC64;
     MAMLYGKHNH EAEEYLEPVF GAPSEQHDLP KYRLPKHSLS PREADRLVRD ELLDEGNSRL
     NLATFCQTYM EPEAVELMKD TLAKNAIDKS EYPRTAEIEN RCVNIIANLW HAPDDEHFTG
     TSTIGSSEAC MLGGLAMKFA WRKRAQAAGL DLNAHRPNLV ISAGYQVCWE KFCVYWDVDI
     HVVPMDEQHM ALDVNHVLDY VDEYTIGIVG IMGITYTGQY DDLAALDKVV THYNHQHPKL
     PVYIHVDAAS GGFYTPFIEP QLIWDFRLAN VVSINASGHK YGLVYPGVGW VVWRDRQFLP
     PELVFKVSYL GGELPTMAIN FSHSAAQLIG QYYNFIRFGM DGYREIQTKT HDVARYLAAA
     LDKVGEFKMI NNGHQLPLIC YQLAPREDRE WTLYDLSDRL LMNGWQVPTY PLPANLEQQV
     IQRIVVRADF GMNMAHDFMD DLTKAVHDLN QAHIVYHHDA APKKYGFTH
//
DBGET integrated database retrieval system