ID   DCEB_LISMO              Reviewed;         464 AA.
AC   Q9EYW9; Q8Y4S0; Q9AGQ0;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Glutamate decarboxylase beta;
DE            Short=GAD-beta;
DE            EC=4.1.1.15;
GN   Name=gadB; OrderedLocusNames=lmo2363;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EGD5, and LO28 / Serovar 1/2c;
RX   PubMed=11309128; DOI=10.1046/j.1365-2958.2001.02398.x;
RA   Cotter P.D., Gahan C.G.M., Hill C.;
RT   "A glutamate decarboxylase system protects Listeria monocytogenes in
RT   gastric fluid.";
RL   Mol. Microbiol. 40:465-475(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- FUNCTION: Converts internalized glutamate to GABA and increases the
CC       internal pH. Involved in glutamate-dependent acid resistance in gastric
CC       fluid.
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   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF309077; AAG22562.1; -; Genomic_DNA.
DR   EMBL; AF329447; AAK17187.1; -; Genomic_DNA.
DR   EMBL; AL591983; CAD00441.1; -; Genomic_DNA.
DR   PIR; AC1370; AC1370.
DR   RefSeq; NP_465886.1; NC_003210.1.
DR   RefSeq; WP_009931286.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q9EYW9; -.
DR   SMR; Q9EYW9; -.
DR   STRING; 169963.lmo2363; -.
DR   PaxDb; Q9EYW9; -.
DR   EnsemblBacteria; CAD00441; CAD00441; CAD00441.
DR   GeneID; 985123; -.
DR   KEGG; lmo:lmo2363; -.
DR   PATRIC; fig|169963.11.peg.2421; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   OMA; TMAPHSE; -.
DR   PhylomeDB; Q9EYW9; -.
DR   BioCyc; LMON169963:LMO2363-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..464
FT                   /note="Glutamate decarboxylase beta"
FT                   /id="PRO_0000146990"
FT   MOD_RES         275
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         92
FT                   /note="A -> P (in strain: LO28)"
FT   VARIANT         124
FT                   /note="E -> D (in strain: LO28)"
FT   VARIANT         261
FT                   /note="F -> L (in strain: EGD5)"
FT   VARIANT         375
FT                   /note="C -> R (in strain: EGD5)"
FT   VARIANT         380..381
FT                   /note="DD -> TT (in strain: LO28)"
SQ   SEQUENCE   464 AA;  53543 MW;  F2E2778CFD1E2C36 CRC64;
     MLYSKENKES YLEPVFGSSA EDRDIPKYTL GKEPLEPRIA YRLVKDELLD EGSARQNLAT
     FCQTYMEDEA TKLMSETLEK NAIDKSEYPR TAELENRCVN IIADLWHAPK DQKFMGTSTI
     GSSEACMLGG MAMKFAWRKR AEKLGLDIYA KKPNLVISSG YQVCWEKFCV YWDIDMRVVP
     MDKEHMQLNT DQVLDYVDEY TIGVVGILGI TYTGRYDDIY ALNEKLEEYN SKTDYKVYIH
     VDAASGGFFT PFVEPDIIWD FRLKNVISIN TSGHKYGLVY PGIGWVLWKD ESYLPEELIF
     KVSYLGGEMP TMQINFSRSA SHIIGQYYNF LRYGFEGYRT IHQKTSDVAQ YLAHAVEQTG
     YFDIFNDGSH LPIVCYKLKD DANVNWTLYD LADRLQMRGW QVPAYPLPKS LENIIIQRYV
     CRADLGFNMA EEFIQDFQAS IQELNNAHIL FHDTQQSGVH GFTH