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Database: UniProt/SWISS-PROT
Entry: DCEB_SHIFL
LinkDB: DCEB_SHIFL
Original site: DCEB_SHIFL 
ID   DCEB_SHIFL              Reviewed;         466 AA.
AC   P69912; P28302; P76873;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   05-DEC-2018, entry version 91.
DE   RecName: Full=Glutamate decarboxylase beta;
DE            Short=GAD-beta;
DE            EC=4.1.1.15;
GN   Name=gadB; OrderedLocusNames=SF1734, S1867;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Converts glutamate to gamma-aminobutyrate (GABA),
CC       consuming one intracellular proton in the reaction. The gad system
CC       helps to maintain a near-neutral intracellular pH when cells are
CC       exposed to extremely acidic conditions. The ability to survive
CC       transit through the acidic conditions of the stomach is essential
CC       for successful colonization of the mammalian host by commensal and
CC       pathogenic bacteria (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   -!- SUBUNIT: Homohexamer composed of three dimers. {ECO:0000250}.
CC   -!- INDUCTION: By acidic conditions. Expression is regulated by a
CC       complex system involving RpoS, cAMP, CRP, EvgAS, H-NS, GadE, GadW
CC       and GadX. The level of involvement for each regulator varies
CC       depending upon the growth phase and the medium (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
DR   EMBL; AE005674; AAN43309.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17196.1; -; Genomic_DNA.
DR   RefSeq; NP_707602.2; NC_004337.2.
DR   RefSeq; WP_000358930.1; NZ_UELP01000115.1.
DR   ProteinModelPortal; P69912; -.
DR   SMR; P69912; -.
DR   EnsemblBacteria; AAN43309; AAN43309; SF1734.
DR   EnsemblBacteria; AAP17196; AAP17196; S1867.
DR   GeneID; 1024938; -.
DR   KEGG; sfl:SF1734; -.
DR   KEGG; sfx:S1867; -.
DR   PATRIC; fig|198214.7.peg.2054; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Acetylation; Complete proteome; Decarboxylase; Lyase;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    466       Glutamate decarboxylase beta.
FT                                /FTId=PRO_0000146985.
FT   REGION      126    127       Pyridoxal phosphate binding.
FT                                {ECO:0000250}.
FT   BINDING      62     62       Substrate. {ECO:0000250}.
FT   BINDING      83     83       Substrate. {ECO:0000250}.
FT   BINDING     212    212       Pyridoxal phosphate. {ECO:0000250}.
FT   BINDING     275    275       Pyridoxal phosphate. {ECO:0000250}.
FT   MOD_RES     276    276       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   MOD_RES     446    446       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     453    453       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     464    464       N6-acetyllysine. {ECO:0000250}.
SQ   SEQUENCE   466 AA;  52668 MW;  8E653330A3C5B4ED CRC64;
     MDKKQVTDLR SELLDSRFGA KSISTIAESK RFPLHEMRDD VAFQIINDEL YLDGNARQNL
     ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC VNMVADLWHA PAPKNGQAVG
     TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK PTDKPNLVCG PVQICWHKFA RYWDVELREI
     PMRPGQLFMD PKRMIEACDE NTIGVVPTFG VTYTGNYEFP QPLHDALDKF QADTGIDIDM
     HIDAASGGFL APFVAPDIVW DFRLPRVKSI SASGHKFGLA PLGCGWVIWR DEEALPQELV
     FNVDYLGGQI GTFAINFSRP AGQVIAQYYE FLRLGREGYT KVQNASYQVA AYLADEIAKL
     GPYEFICTGR PDEGIPAVCF KLKDGEDPGY TLYDLSERLR LRGWQVPAFT LGGEATDIVV
     MRIMCRRGFE MDFAELLLED YKASLKYLSD HPKLQGIAQQ NSFKHT
//
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