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 03-AUG-2022, entry version 106.
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., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., 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., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Converts glutamate to gamma-aminobutyrate (GABA), consuming
CC one intracellular proton in the reaction. The gad system helps to
CC maintain a near-neutral intracellular pH when cells are exposed to
CC extremely acidic conditions. The ability to survive transit through the
CC acidic conditions of the stomach is essential for successful
CC colonization of the mammalian host by commensal and pathogenic bacteria
CC (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 complex
CC system involving RpoS, cAMP, CRP, EvgAS, H-NS, GadE, GadW and GadX. The
CC level of involvement for each regulator varies depending upon the
CC growth phase and the medium (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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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_WHSI01000051.1.
DR AlphaFoldDB; P69912; -.
DR SMR; P69912; -.
DR STRING; 198214.SF1734; -.
DR PRIDE; P69912; -.
DR EnsemblBacteria; AAN43309; AAN43309; SF1734.
DR EnsemblBacteria; AAP17196; AAP17196; S1867.
DR GeneID; 1024938; -.
DR GeneID; 66674655; -.
DR KEGG; sfl:SF1734; -.
DR KEGG; sfx:S1867; -.
DR PATRIC; fig|198214.7.peg.2054; -.
DR HOGENOM; CLU_019582_0_0_6; -.
DR OMA; TMAPHSE; -.
DR OrthoDB; 1478871at2; -.
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; Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..466
FT /note="Glutamate decarboxylase beta"
FT /id="PRO_0000146985"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126..127
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 276
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 453
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 464
FT /note="N6-acetyllysine"
FT /evidence="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
