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 27-MAR-2024, entry version 109. 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; Bacillota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; llm:llmg_1179; -. DR eggNOG; COG0076; Bacteria. DR HOGENOM; CLU_019582_2_1_9; -. DR OrthoDB; 9803665at2; -. DR PhylomeDB; O30418; -. DR Proteomes; UP000000364; 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; 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 //