ID   DCE_LACLA               Reviewed;         466 AA.
AC   Q9CG20; O50645;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Glutamate decarboxylase;
DE            Short=GAD;
DE            EC=4.1.1.15;
GN   Name=gadB; OrderedLocusNames=LL1290; ORFNames=L123581;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, AND
RP   CHARACTERIZATION.
RC   STRAIN=01-7;
RX   PubMed=10411264; DOI=10.1099/13500872-145-6-1375;
RA   Nomura M., Nakajima I., Fujita Y., Kobayashi M., Kimoto H., Suzuki I.,
RA   Aso H.;
RT   "Lactococcus lactis contains only one glutamate decarboxylase gene.";
RL   Microbiology 145:1375-1380(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Converts internalized glutamate to GABA and increases the
CC       internal pH. Involved in glutamate-dependent acid resistance (By
CC       similarity). {ECO:0000250}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.7. Active at acidic pHs but inactive in the neutral
CC         pH range.;
CC       Temperature dependence:
CC         Active up to 70 degrees Celsius at pH 4.1.;
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AB010789; BAA24585.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK05388.1; -; Genomic_DNA.
DR   PIR; B86786; B86786.
DR   RefSeq; NP_267446.1; NC_002662.1.
DR   RefSeq; WP_010905870.1; NC_002662.1.
DR   AlphaFoldDB; Q9CG20; -.
DR   SMR; Q9CG20; -.
DR   PaxDb; 272623-L123581; -.
DR   EnsemblBacteria; AAK05388; AAK05388; L123581.
DR   KEGG; lla:L123581; -.
DR   PATRIC; fig|272623.7.peg.1393; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000002196; 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   CDD; cd06450; DOPA_deC_like; 1.
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   1: Evidence at protein level;
KW   Decarboxylase; Direct protein sequencing; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..466
FT                   /note="Glutamate decarboxylase"
FT                   /id="PRO_0000146986"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  53927 MW;  BCDC732253E473C2 CRC64;
     MLYGKENRDE AEFLEPIFGS ESEQVDLPKY KLAQQSIEPR VAYQLVQDEM LDEGNARLNL
     ATFCQTYMEP EAVKLMSQTL EKNAIDKSEY PRTTEIENRC VNMIADLWNA SEKEKFMGTS
     TIGSSEACML GGMAMKFSWR KRAEKLGLDI NAKKPNLVIS SGYQVCWEKF CIYWDIEMRE
     VPMDKEHMSI NLDKVMDYVD EYTIGVVGIM GITYTGRYDD IKALDNLIEE YNKQTDYKVY
     IHVDAASGGL YAPFVEPELE WDFRLKNVIS INTSGHKYGL VYPGVGWVLW RDKKYLPEEL
     IFKVSYLGGE LPTMAINFSH SASQLIGQYY NFVRYGFDGY KAIHERTHKV AMFLAKEIEK
     TGMFEIMNDG SQLPIVCYKL KEDSNRGWNL YDLADRLLMK GWQVPAYPLP KNLENEIIQR
     LVIRADFGMN MAFNYVQDMQ EAIEALNKAH ILYHEEPENK TYGFTH
//