ID   DCE_LACLM               Reviewed;         466 AA.
AC   O30418; A2RKG2;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Glutamate decarboxylase;
DE            EC=4.1.1.15;
GN   Name=gadB; OrderedLocusNames=llmg_1179;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=9484886; DOI=10.1046/j.1365-2958.1998.00676.x;
RA   Sanders J.W., Leenhouts K., Burghoorn J., Brands J.R., Venema G., Kok J.;
RT   "A chloride-inducible acid resistance mechanism in Lactococcus lactis and
RT   its regulation.";
RL   Mol. Microbiol. 27:299-310(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- FUNCTION: Converts internalized glutamate to GABA and increases the
CC       internal pH. Involved in glutamate-dependent acid resistance.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- INDUCTION: Expression is highest at onset of stationary phase in
CC       presence of NaCl and glutamate, and at low pH. Chloride-dependent
CC       expression is activated by GadR.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF005098; AAC46188.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97772.1; -; Genomic_DNA.
DR   RefSeq; WP_011835080.1; NZ_WJVF01000010.1.
DR   AlphaFoldDB; O30418; -.
DR   SMR; O30418; -.
DR   STRING; 416870.llmg_1179; -.
DR   EnsemblBacteria; CAL97772; CAL97772; llmg_1179.
DR   KEGG; llm:llmg_1179; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   OMA; TMAPHSE; -.
DR   PhylomeDB; O30418; -.
DR   BioCyc; LLAC416870:LLMG_RS05970-MON; -.
DR   Proteomes; UP000000364; 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   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..466
FT                   /note="Glutamate decarboxylase"
FT                   /id="PRO_0000146987"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        114
FT                   /note="E -> G (in Ref. 1; AAC46188)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116..117
FT                   /note="FM -> IY (in Ref. 1; AAC46188)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   466 AA;  53924 MW;  668DB73A4DF40BF9 CRC64;
     MLYGKENRDE AEFLEPIFGS ESEQVDLPKY KLAQQSIEPR VAYQLVQDEM LDEGNARLNL
     ATFCQTYMEP EAVKLMSQTL EKNAIDKSEY PRTTEIENRC VNMIADLWNA SEKEKFMGTS
     TIGSSEACML GGMAMKFSWR KRAEKLGLDI NAKKPNLVIS SGYQVCWEKF CVYWDIEMRE
     VPMDREHMSI NLEKVMDYVD EYTIGVVGIM GITYTGRYDD IKALDNLIEE YNKQTDYKVY
     IHVDAASGGL YAPFVEPELE WDFRLKNVIS INTSGHKYGL VYPGVGWVLW RDKKYLPEEL
     IFKVSYLGGE LPTMAINFSH SASQLIGQYY NFVRYGFDGY KAIHERTHKV AMYLAEEIEK
     TGMFEIMNDG AQLPIVCYKL KENSNRGWNL YDLADRLLMK GWQVPAYPLP KNLENEIIQR
     LVIRADFGMN MAFNYVQDMQ EAIDALNKAH ILFHQEPENK TYGFTH