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Database: UniProt/SWISS-PROT
Entry: DCEB_ECOL6
LinkDB: DCEB_ECOL6
Original site: DCEB_ECOL6 
ID   DCEB_ECOL6              Reviewed;         466 AA.
AC   Q8FHG5;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   07-JUN-2017, entry version 89.
DE   RecName: Full=Glutamate decarboxylase beta;
DE            Short=GAD-beta;
DE            EC=4.1.1.15;
GN   Name=gadB; OrderedLocusNames=c1922;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN80380.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE014075; AAN80380.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000358860.1; NC_004431.1.
DR   ProteinModelPortal; Q8FHG5; -.
DR   SMR; Q8FHG5; -.
DR   STRING; 199310.c1922; -.
DR   PRIDE; Q8FHG5; -.
DR   EnsemblBacteria; AAN80380; AAN80380; c1922.
DR   KEGG; ecc:c1922; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000001410; 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   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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.
FT   CHAIN         1    466       Glutamate decarboxylase beta.
FT                                /FTId=PRO_0000146983.
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;  52653 MW;  C953BB99AAF48923 CRC64;
     MDKKQVTDLR SELLDSRFGA KSISTIAESK RFPLHEMRDD VAFQIINDEL YLDGNARQNL
     ATFCQTWDDD NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC VNMVADLWHA PAPKNGQAVG
     TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK PTNKPNLVCG 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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