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
//
