ID   DCEA_LISMO              Reviewed;         462 AA.
AC   Q9F5P3; Q8Y9S6;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Glutamate decarboxylase alpha;
DE            Short=GAD-alpha;
DE            EC=4.1.1.15;
GN   Name=gadA; OrderedLocusNames=lmo0447;
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=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; AF309076; AAG22560.1; -; Genomic_DNA.
DR   EMBL; AL591975; CAC98526.1; -; Genomic_DNA.
DR   PIR; AH1130; AH1130.
DR   RefSeq; NP_463976.1; NC_003210.1.
DR   RefSeq; WP_010989470.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q9F5P3; -.
DR   SMR; Q9F5P3; -.
DR   STRING; 169963.lmo0447; -.
DR   PaxDb; Q9F5P3; -.
DR   EnsemblBacteria; CAC98526; CAC98526; CAC98526.
DR   GeneID; 986724; -.
DR   KEGG; lmo:lmo0447; -.
DR   PATRIC; fig|169963.11.peg.462; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   OMA; RHINAEE; -.
DR   PhylomeDB; Q9F5P3; -.
DR   BioCyc; LMON169963:LMO0447-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..462
FT                   /note="Glutamate decarboxylase alpha"
FT                   /id="PRO_0000146988"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        152
FT                   /note="S -> N (in Ref. 1; AAG22560)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  52498 MW;  EA1A442E3E1CE2FA CRC64;
     MFKTNVEQNN VPVFGSFESG QDLPEKRMNK ESVDPRIAYQ LVKDQLIDEG SARQNLATFC
     QTYMEPEAEQ IMAETMEKNA IDKSEYPQTA KLESSCVNML ADLWNVDESE HYMGTSTVGS
     SEACMLGGMA MKFRWRSAAL KNGLDIHAKK PSLVISSGYQ VCWEKFCVYW DIELREVPMS
     EEHLSINTDI IMDYVDEYTI GIVGILGITY TGKFDDIMTL NDLVEDYNNT HDNEVVIHVD
     GASGAMFTPF VEPGLEWDFR LPNVVSINTS GHKYGLVYPG VGWILWRDKE YLPEELVFDV
     SYLGGHMPTM AINFSRSASQ IIGQYYNFLR FGYEGYRQIH MRTRDGALQL SQAVAETGLF
     EIYNDGANLP IVCYKLKDDA NVAWTLYDLA DRLQMKGWQV PAYPLPKEMG NTIIQRYVCR
     GDLGQNMVTA FKNDLSESIE ELNNAHILYH DVNTSKTHGF TH