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Database: UniProt/TrEMBL
Entry: A0A1V0BEH5_9BURK
LinkDB: A0A1V0BEH5_9BURK
Original site: A0A1V0BEH5_9BURK 
ID   A0A1V0BEH5_9BURK        Unreviewed;       459 AA.
AC   A0A1V0BEH5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   30-AUG-2017, entry version 3.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=B5M06_08820 {ECO:0000313|EMBL:AQZ98339.1};
OS   Comamonas kerstersii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=225992 {ECO:0000313|EMBL:AQZ98339.1};
RN   [1] {ECO:0000313|EMBL:AQZ98339.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=8943 {ECO:0000313|EMBL:AQZ98339.1};
RA   Zheng B.;
RT   "Rapid Whole Genome Sequencing of Comamonas kerstersii Causing
RT   Continuous ambulatory Peritoneal Dialysis-Associated Peritonitis.";
RL   Submitted (MAR-2017) 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; CP020121; AQZ98339.1; -; Genomic_DNA.
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   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     266    266       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   459 AA;  51772 MW;  3AFB01D4184C450B CRC64;
     MAQNLNDDIY ASRELLSSLP KKRFPENELN GRNVFSAVRD ELMLDGNSRQ NLATFCQTWV
     DDYARAIMDL SIDKNMIDKD EYPQTAEIES RCVHMLADLW NSPSPETTLG CSTVGSSEAA
     MLGGLALKWQ WRKKRAAQGK STDRPNMVCG PVQICWHKFA RYFDVEIREV PLEGDRMIMN
     PDEVLKRVDE NTIGVVPTMG VTFTCQYEPV KAIHDALDKL QQETGLDIPM HVDGASGGFL
     APFCAPEIEW DFRLPRVKSI NSSGHKFGLA PLGVGWVIWR EAKDLPEELI FNVNYLGGNM
     PTFALNFSRP GGQVIAQYYN FLRLGREGYA KVHGACYETA MYLAKEIEKL GDFKIIFDGN
     PKHGIPALAW TLKNPDAING YTLYDFADRL RSRGWQVPAY SMPANREDLV VQRILVRHGV
     SRDLGSLLIE DMKRALEYFK AHPVSNPLTE KEAGGFSHR
//
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