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Database: UniProt/TrEMBL
Entry: A0A157PMR9_9BORD
LinkDB: A0A157PMR9_9BORD
Original site: A0A157PMR9_9BORD 
ID   A0A157PMR9_9BORD        Unreviewed;       466 AA.
AC   A0A157PMR9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-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   Name=gadA2 {ECO:0000313|EMBL:SAI69978.1};
GN   ORFNames=SAMEA3906487_02011 {ECO:0000313|EMBL:SAI69978.1};
OS   Bordetella trematum.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI69978.1, ECO:0000313|Proteomes:UP000076825};
RN   [1] {ECO:0000313|EMBL:SAI69978.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H044680328 {ECO:0000313|EMBL:SAI69978.1};
RG   Pathogen Informatics;
RL   Submitted (APR-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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; LT546645; SAI69978.1; -; Genomic_DNA.
DR   RefSeq; WP_063491883.1; NZ_LT546645.1.
DR   EnsemblBacteria; SAI69978; SAI69978; SAMEA3906487_02011.
DR   KEGG; btrm:SAMEA390648702011; -.
DR   PATRIC; fig|123899.6.peg.2006; -.
DR   KO; K01580; -.
DR   Proteomes; UP000076825; 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:UP000076825};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:SAI69978.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076825}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   466 AA;  52411 MW;  1C6808562DE3B95F CRC64;
     MPLHAKDTVR ADLLDDVYAS SDLSVAMPKY KLPAEGHAPR HAYQVVHDEL MLDGNSRQNL
     ATFCQTWVDE EVHKLMDESI DKNMIDKDEY PQTAEIEARC VHMIADLWHS PDAMNTLGCS
     TTGSSEAAML GGLAMKWAWR KKRQAAGLPT DRPNLICGPV QICWHKFARY FDVELREIPM
     EQDRLIMSPE EVIKRCDENT IGVVPTLGVT FSCDYEPVKA VHDALDKLQQ DTGLDIPIHV
     DGASGGFLAP FCAPDLEWDF RLPRVVSINT SGHKFGLAPL GVGWIVWRDA AHLPEELIFD
     VNYLGGNMPT FALNFSRPGG QIVAQYYNFL RLGREGYTRI QQACYDTAQY LADEIARLGP
     FEMLFDGNPQ KGIPALCWKI KDGQKDLGFN LYDLADRLRS RGWQVPAYSM PAHREDLVVQ
     RILVRHGVSR DLASLLIEDF KRALAYFARH PVAVQGSEDE SGGFHH
//
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