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Database: UniProt/SWISS-PROT
Entry: DCEB_LISIN
LinkDB: DCEB_LISIN
Original site: DCEB_LISIN 
ID   DCEB_LISIN              Reviewed;         464 AA.
AC   Q928R9;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   05-DEC-2018, entry version 88.
DE   RecName: Full=Glutamate decarboxylase beta;
DE            Short=GAD-beta;
DE            EC=4.1.1.15;
GN   Name=gadB; OrderedLocusNames=lin2463;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
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 (By 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   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
DR   EMBL; AL596172; CAC97690.1; -; Genomic_DNA.
DR   PIR; AB1740; AB1740.
DR   RefSeq; WP_010991206.1; NC_003212.1.
DR   ProteinModelPortal; Q928R9; -.
DR   SMR; Q928R9; -.
DR   STRING; 272626.lin2463; -.
DR   EnsemblBacteria; CAC97690; CAC97690; CAC97690.
DR   KEGG; lin:lin2463; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000002513; 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.
FT   CHAIN         1    464       Glutamate decarboxylase beta.
FT                                /FTId=PRO_0000146989.
FT   MOD_RES     275    275       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   464 AA;  53600 MW;  4C35CD1395ADF481 CRC64;
     MLYSKENKES YLEPVFGSSA EDRDIPKYTL AKEPLEPRIA YRLVKDELLD EGSARQNLAT
     FCQTYMEDEA TKLMSETLEK NAIDKSEYPR TAELENRCVN IIADLWHAPK DQKFMGTSTI
     GSSEACMLGG MAMKFAWRKR AEKLGLDIYA QKPNLVISSG YQVCWEKFCV YWDIDMRVVP
     MDKDHMQLNT DQVLDYVDEY TIGVVGILGI TYTGRYDDIY ALNEKLEEYN SKTDYKVYIH
     VDAASGGFFT PFVEPDIIWD FRLKNVISIN TSGHKYGLVY PGIGWVLWKD ESYLPEELIF
     KVSYLGGEMP TMQINFSRSA SHIIGQYYNF LRYGFEGYRT IHQKTSDVAQ YLAHAVEQTG
     YFDIYNDGSH LPIVCYKLKD DANVKWTLYD LADRLQMRGW QVPAYPLPKN LENIIIQRYV
     CRADLGFNMA EEFIQDFQAS IQELNNAHIL FHDTQQSGVH GFTH
//
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