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Database: UniProt/TrEMBL
Entry: E3PMA7_ECOH1
LinkDB: E3PMA7_ECOH1
Original site: E3PMA7_ECOH1 
ID   E3PMA7_ECOH1            Unreviewed;       466 AA.
AC   E3PMA7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   20-DEC-2017, entry version 38.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=ETEC_3763 {ECO:0000313|EMBL:CBJ03264.1};
OS   Escherichia coli O78:H11 (strain H10407 / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316401 {ECO:0000313|EMBL:CBJ03264.1, ECO:0000313|Proteomes:UP000006877};
RN   [1] {ECO:0000313|EMBL:CBJ03264.1, ECO:0000313|Proteomes:UP000006877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H10407 / ETEC {ECO:0000313|Proteomes:UP000006877};
RX   PubMed=20802035; DOI=10.1128/JB.00710-10;
RA   Crossman L.C., Chaudhuri R.R., Beatson S.A., Wells T.J., Desvaux M.,
RA   Cunningham A.F., Petty N.K., Mahon V., Brinkley C., Hobman J.L.,
RA   Savarino S.J., Turner S.M., Pallen M.J., Penn C.W., Parkhill J.,
RA   Turner A.K., Johnson T.J., Thomson N.R., Smith S.G., Henderson I.R.;
RT   "A commensal gone bad: complete genome sequence of the prototypical
RT   enterotoxigenic Escherichia coli strain H10407.";
RL   J. Bacteriol. 192:5822-5831(2010).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; FN649414; CBJ03264.1; -; Genomic_DNA.
DR   RefSeq; WP_000372266.1; NC_017633.1.
DR   EnsemblBacteria; CBJ03264; CBJ03264; ETEC_3763.
DR   KEGG; elh:ETEC_3763; -.
DR   KO; K01580; -.
DR   OMA; FTTSVYG; -.
DR   Proteomes; UP000006877; 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   Complete proteome {ECO:0000313|Proteomes:UP000006877};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     276    276       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   466 AA;  52675 MW;  F468B3E7DF542122 CRC64;
     MDQKLLTDFR SELLDSRFGA KAISTIAESK RFPLHEMRDD VAFQIINDEL YLDGNARQNL
     ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY SQSAAIDLRC 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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