ID   F9UU99_LACPL            Unreviewed;       469 AA.
AC   F9UU99;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   Name=gadB {ECO:0000313|EMBL:CCC80401.1};
GN   OrderedLocusNames=lp_3420 {ECO:0000313|EMBL:CCC80401.1};
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC80401.1, ECO:0000313|Proteomes:UP000000432};
RN   [1] {ECO:0000313|EMBL:CCC80401.1, ECO:0000313|Proteomes:UP000000432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC   {ECO:0000313|Proteomes:UP000000432};
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W.,
RA   Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R.,
RA   de Vries M., Ursing B., de Vos W.M., Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2] {ECO:0000313|EMBL:CCC80401.1, ECO:0000313|Proteomes:UP000000432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC   {ECO:0000313|Proteomes:UP000000432};
RX   PubMed=22156394; DOI=10.1128/JB.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.F.T.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00000018,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; AL935263; CCC80401.1; -; Genomic_DNA.
DR   RefSeq; YP_004890915.1; NC_004567.2.
DR   AlphaFoldDB; F9UU99; -.
DR   SMR; F9UU99; -.
DR   STRING; 220668.lp_3420; -.
DR   EnsemblBacteria; CCC80401; CCC80401; lp_3420.
DR   KEGG; lpl:lp_3420; -.
DR   PATRIC; fig|220668.9.peg.2850; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   OrthoDB; 9803665at2; -.
DR   PhylomeDB; F9UU99; -.
DR   Proteomes; UP000000432; Chromosome.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
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; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000432}.
FT   MOD_RES         280
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   469 AA;  53574 MW;  1C54E6A1BAF4C3D9 CRC64;
     MAMLYGKHNH EAEEYLEPVF GAPSEQHDLP KYRLPKHSLS PREADRLVRD ELLDEGNSRL
     NLATFCQTYM EPEAVELMKD TLAKNAIDKS EYPRTAEIEN RCVNIIANLW HAPDDEHFTG
     TSTIGSSEAC MLGGLAMKFA WRKRAQAAGL DLNAHRPNLV ISAGYQVCWE KFCVYWDVDM
     HVVPMDEQHM ALDVNHVLDY VDEYTIGIVG IMGITYTGQY DDLAALDKVV THYNHQHPKL
     PVYIHVDAAS GGFYTPFIEP QLIWDFRLAN VVSINASGHK YGLVYPGVGW VVWRDRQFLP
     PELVFKVSYL GGELPTMAIN FSHSAAQLIG QYYNFIRFGM DGYREIQTKT HDVARYLAAA
     LDKVGEFKMI NNGHQLPLIC YQLASREDRE WTLYDLSDRL LMNGWQVPTY PLPANLEQQV
     IQRIVVRADF GMNMAHDFMD DLTKAVHDLN HAHIVYHHDA APKKYGFTH
//