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Database: UniProt/TrEMBL
Entry: A0A1D8ILM3_9GAMM
LinkDB: A0A1D8ILM3_9GAMM
Original site: A0A1D8ILM3_9GAMM 
ID   A0A1D8ILM3_9GAMM        Unreviewed;       457 AA.
AC   A0A1D8ILM3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   25-OCT-2017, entry version 8.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=BI364_04395 {ECO:0000313|EMBL:AOU97331.1};
OS   Acidihalobacter prosperus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=160660 {ECO:0000313|EMBL:AOU97331.1, ECO:0000313|Proteomes:UP000095401};
RN   [1] {ECO:0000313|EMBL:AOU97331.1, ECO:0000313|Proteomes:UP000095401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F5 {ECO:0000313|EMBL:AOU97331.1,
RC   ECO:0000313|Proteomes:UP000095401};
RA   Khaleque H.N., Ramsay J.P., Kaksonen A.H., Boxall N.J., Watkin E.L.J.;
RT   "Acidihalobacter prosperus F5.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP017415; AOU97331.1; -; Genomic_DNA.
DR   RefSeq; WP_070077718.1; NZ_CP017415.1.
DR   EnsemblBacteria; AOU97331; AOU97331; BI364_04395.
DR   KEGG; aprs:BI364_04395; -.
DR   KO; K01580; -.
DR   Proteomes; UP000095401; 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   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000095401};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     272    272       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   457 AA;  51189 MW;  5B10E066DFFEC887 CRC64;
     MVKKLLPDTD LAPTYGSRAM SEPVPKYALP DGEMAPQTAY QLIHDELMLD GNARLNLATF
     VTTWMEPEAE RLMAETFDKN MIDKDEYPQT AEIETRCVNM IARLFNVPDD GAAVGVSAIG
     SSEAVMLAGM ALKWRWRARR EASGKSADKP NLILGANVQV VWEKFCRYWE VEPRYIPMRE
     GRYVITPEEV LERIDENTIG IVAILGTTFT GEFEPIEAIH DAVVAHNKTH GLVVPLHIDA
     ASGGFVAPFI HPDLRWDFRL PNVVSINASG HKYGLVYPGV GWAVWRSQEH LPEDLVFHVN
     YLGGDMPTFT LNFSRPGNQI VGQYYNFLRL GRKGYTRIMS TLRDTATELA ARISKLGPFD
     LLSDGSAIPV FAFRLKDASR YSVYDVSERL RIRGWQVPAY TMPPEAQNIA VLRVVIREGF
     SRDMADLLLN DLSKVVDELS ASPPTHPKTA DGRFHHG
//
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