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Database: UniProt/TrEMBL
Entry: A0A160FSU9_9BURK
LinkDB: A0A160FSU9_9BURK
Original site: A0A160FSU9_9BURK 
ID   A0A160FSU9_9BURK        Unreviewed;       461 AA.
AC   A0A160FSU9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   20-JUN-2018, entry version 16.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AYM40_28415 {ECO:0000313|EMBL:ANB76189.1};
OS   Burkholderia sp. OLGA172.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1804984 {ECO:0000313|EMBL:ANB76189.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB76189.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB76189.1,
RC   ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
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; CP014579; ANB76189.1; -; Genomic_DNA.
DR   RefSeq; WP_063499435.1; NZ_CP014579.1.
DR   EnsemblBacteria; ANB76189; ANB76189; AYM40_28415.
DR   KEGG; buz:AYM40_28415; -.
DR   KO; K01580; -.
DR   Proteomes; UP000076852; Chromosome 2.
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   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:UP000076852};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076852}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   461 AA;  51268 MW;  4545CA40548AED88 CRC64;
     MTFLKSPPST PDAVADEYAA TISGSSLPKY RIPETSSDRR AVFDLVRDEL FMDGNSRQNV
     ATFCTTYADD EVRRLMDLSI DKNMIDKDEY PQTAEIEMRC VHMLADLWHA TKSWKTTGCS
     TTGSSEACML GGLALKWQWK KRRQAQGKPT DKPNFVCGPV QVCWAKFARY FDVEMRQVPL
     SGDATGLRPE DLAQYCDENT IGVVATLGIT FTCVYEPVKA LAGALDALQA NVGLDIPIHV
     DAASGGFVAP FIQPDLEWDF SVPRVKSINA SGHKYGLAPL GVGWVVWRST QELPDELIFR
     VDYLGGDMPT FALNFSRPAG QIIAQYYMLL RLGREGYRHI QQECADTAQA LADGLAKIDA
     LEMIYDGRGA LPAVCYKLKR PETAGFTLFD LSDQVRMRGW QIASYELPAG REDTIVQRVL
     IRRGVTRDMT AMLLEDIRHA VAHLTKNPVL HSTAGPTFHH D
//
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