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Database: UniProt/SWISS-PROT
Entry: DCEA_LISMO
LinkDB: DCEA_LISMO
Original site: DCEA_LISMO 
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   20-JUN-2018, entry version 96.
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.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA   Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA   Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA   Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA   Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA   Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   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
CC       the internal pH. Involved in glutamate-dependent acid resistance
CC       in gastric fluid.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
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}.
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; NC_003210.1.
DR   ProteinModelPortal; 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; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; STFRMPE; -.
DR   PhylomeDB; Q9F5P3; -.
DR   BioCyc; LMON169963:LMO0447-MONOMER; -.
DR   Proteomes; UP000000817; 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   3: Inferred from homology;
KW   Complete proteome; Decarboxylase; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    462       Glutamate decarboxylase alpha.
FT                                /FTId=PRO_0000146988.
FT   MOD_RES     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   CONFLICT    152    152       S -> N (in Ref. 1; AAG22560).
FT                                {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
//
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