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Database: UniProt/TrEMBL
Entry: A0A0B6RZ20_BURGL
LinkDB: A0A0B6RZ20_BURGL
Original site: A0A0B6RZ20_BURGL 
ID   A0A0B6RZ20_BURGL        Unreviewed;       447 AA.
AC   A0A0B6RZ20;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUL-2017, entry version 20.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gad {ECO:0000313|EMBL:AJK45246.1};
GN   ORFNames=BGL_1c07110 {ECO:0000313|EMBL:AJK45246.1};
OS   Burkholderia glumae PG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=595500 {ECO:0000313|EMBL:AJK45246.1, ECO:0000313|Proteomes:UP000031838};
RN   [1] {ECO:0000313|Proteomes:UP000031838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1 {ECO:0000313|Proteomes:UP000031838};
RA   Voget S., Streit W.R., Jaeger K.E., Daniel R.;
RL   Submitted (MAR-2011) 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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP002580; AJK45246.1; -; Genomic_DNA.
DR   RefSeq; WP_042624009.1; NZ_CP002580.1.
DR   EnsemblBacteria; AJK45246; AJK45246; BGL_1c07110.
DR   KEGG; bgp:BGL_1c07110; -.
DR   KO; K01580; -.
DR   Proteomes; UP000031838; 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:UP000031838};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:AJK45246.1};
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;  49669 MW;  D51517C9A452B077 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 GIHHRFTLYD LSDRMRMRGW QIASYPLPAN RQDVIVQRVL
     IRHGISRDLI KILLDDLHKA IEYLQGN
//
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