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Database: UniProt/TrEMBL
Entry: A0A0P0KK22_9BURK
LinkDB: A0A0P0KK22_9BURK
Original site: A0A0P0KK22_9BURK 
ID   A0A0P0KK22_9BURK        Unreviewed;       447 AA.
AC   A0A0P0KK22;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-JUL-2017, entry version 13.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=bpln_1g07010 {ECO:0000313|EMBL:ALK29526.1};
OS   Burkholderia plantarii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=41899 {ECO:0000313|EMBL:ALK29526.1};
RN   [1] {ECO:0000313|EMBL:ALK29526.1, ECO:0000313|Proteomes:UP000065964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43733 {ECO:0000313|EMBL:ALK29526.1,
RC   ECO:0000313|Proteomes:UP000065964};
RX   PubMed=25943361; DOI=10.1186/s12864-015-1558-5;
RA   Seo Y.S., Lim J.Y., Park J., Kim S., Lee H.H., Cheong H., Kim S.M.,
RA   Moon J.S., Hwang I.;
RT   "Comparative genome analysis of rice-pathogenic Burkholderia provides
RT   insight into capacity to adapt to different environments and hosts.";
RL   BMC Genomics 16:349-349(2015).
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; CP007212; ALK29526.1; -; Genomic_DNA.
DR   RefSeq; WP_055138103.1; NZ_MKGK01000006.1.
DR   EnsemblBacteria; ALK29526; ALK29526; bpln_1g07010.
DR   KEGG; bpla:bpln_1g07010; -.
DR   PATRIC; fig|41899.3.peg.772; -.
DR   KO; K01580; -.
DR   Proteomes; UP000065964; Chromosome 1.
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:UP000065964};
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     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   447 AA;  49647 MW;  DE5E57C2EF12B077 CRC64;
     MKIELPEREI NGELGGIYSA HVSQHPLPTL RIPDTSTAPA VAYNLIHDEL LLDGNSQQNL
     ATFCTTWVEP EVQQLMTDAI DKNMIDKDEY PQTAEIENRC VTMIADLWHA PDPLGTIGCS
     TTGSSEACML GGLALKWKWK QRREAAGLST ARPNFVCGPV QICWKKFARY FDVEIREAPL
     HGDGLGITPA DLRELCDENT IGVVATLGVT FTGIYEPVAA LAAELDAMQR ELGLDIPIHV
     DAASGGFVAP FIQPDLEWDF SIERVKSINA SGHKYGLAPL GVGWAVWRSK QELPEDLIFY
     VDYLGGNMAT FALNFSRPGG EIIAQYYNFL RLGREGYTGI QQACSDTAQW LAAEVARLGP
     LELVYDGRGG LPAVCYRLKD GIDHRFTLYD LSDRMRMRGW QIASYPLPAN RQDVIVQRVL
     IRHGISRDLI KILLDDLHKA IEYLQGN
//
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