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Database: UniProt/SWISS-PROT
Entry: DCEA_SHIFL
LinkDB: DCEA_SHIFL
Original site: DCEA_SHIFL 
ID   DCEA_SHIFL              Reviewed;         466 AA.
AC   Q83PR1; Q7UAY1;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   12-SEP-2018, entry version 95.
DE   RecName: Full=Glutamate decarboxylase alpha;
DE            Short=GAD-alpha;
DE            EC=4.1.1.15;
GN   Name=gadA; OrderedLocusNames=SF3594, S4173;
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: L-glutamate = 4-aminobutanoate + CO(2).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homohexamer. {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; AAN45045.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19142.1; -; Genomic_DNA.
DR   RefSeq; NP_709338.2; NC_004337.2.
DR   RefSeq; WP_000372244.1; NZ_MTPK01000136.1.
DR   ProteinModelPortal; Q83PR1; -.
DR   SMR; Q83PR1; -.
DR   PRIDE; Q83PR1; -.
DR   EnsemblBacteria; AAN45045; AAN45045; SF3594.
DR   EnsemblBacteria; AAP19142; AAP19142; S4173.
DR   GeneID; 1026324; -.
DR   KEGG; sfl:SF3594; -.
DR   KEGG; sfx:S4173; -.
DR   PATRIC; fig|198214.7.peg.4243; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; FTTSVYG; -.
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   Complete proteome; Decarboxylase; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    466       Glutamate decarboxylase alpha.
FT                                /FTId=PRO_0000146981.
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}.
SQ   SEQUENCE   466 AA;  52700 MW;  44B04876B2DF1680 CRC64;
     MDQKLLTDFR SELLDSRFGA KAISTIAESK 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 AYLADEIAKQ
     GPYEFICTGR PDEGIPAVCF KLKDGEDPGY TLYDLSERLR LRGWQVPAFT LGGEATDIVV
     MRIMCRRGFE MDFAELLLED YKASLKYLSD HPKLQGIAQQ NSFKHT
//
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