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Database: UniProt/TrEMBL
Entry: A0A0H2Z472_ECOK1
LinkDB: A0A0H2Z472_ECOK1
Original site: A0A0H2Z472_ECOK1 
ID   A0A0H2Z472_ECOK1        Unreviewed;       476 AA.
AC   A0A0H2Z472;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   25-APR-2018, entry version 18.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gadB {ECO:0000313|EMBL:ABJ02999.1};
GN   ORFNames=APECO1_2931 {ECO:0000313|EMBL:ABJ02999.1};
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955 {ECO:0000313|EMBL:ABJ02999.1, ECO:0000313|Proteomes:UP000008216};
RN   [1] {ECO:0000313|EMBL:ABJ02999.1, ECO:0000313|Proteomes:UP000008216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APEC O1 {ECO:0000313|EMBL:ABJ02999.1};
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ02999.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABJ02999; ABJ02999; APECO1_2931.
DR   KEGG; ecv:APECO1_2931; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000008216; 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 {ECO:0000313|Proteomes:UP000008216};
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     286    286       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   476 AA;  53823 MW;  8987B0B94BC1AC9C CRC64;
     MXSNXFKEFX MDXKXXTDXX SELLDSRFGA KXISTIAESK RFPLHEMRDD VAFQIINDEL
     YLDGNARQNL ATFCQTWDDX 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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