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Database: UniProt/TrEMBL
Entry: A0A097EPN3_9GAMM
LinkDB: A0A097EPN3_9GAMM
Original site: A0A097EPN3_9GAMM 
ID   A0A097EPN3_9GAMM        Unreviewed;       448 AA.
AC   A0A097EPN3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   20-DEC-2017, entry version 18.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=LO80_05800 {ECO:0000313|EMBL:AIT09528.1};
OS   Francisella sp. FSC1006.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=1547445 {ECO:0000313|EMBL:AIT09528.1, ECO:0000313|Proteomes:UP000029672};
RN   [1] {ECO:0000313|EMBL:AIT09528.1, ECO:0000313|Proteomes:UP000029672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC1006 {ECO:0000313|EMBL:AIT09528.1,
RC   ECO:0000313|Proteomes:UP000029672};
RA   Granberg M., Backman S., Lundmark E., Nilsson E., Karlsson E.,
RA   Thelaus J., Ohrman C., Larkeryd A., Stenberg P.;
RT   "Whole genome sequence of Francisella endociliophora strain FSC1006,
RT   isolated from a laboratory culture of the marine ciliate Euplotes
RT   raikovi.";
RL   Submitted (OCT-2014) 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; CP009574; AIT09528.1; -; Genomic_DNA.
DR   RefSeq; WP_040009429.1; NZ_CP009574.1.
DR   EnsemblBacteria; AIT09528; AIT09528; LO80_05800.
DR   KEGG; frf:LO80_05800; -.
DR   KO; K01580; -.
DR   Proteomes; UP000029672; Chromosome.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029672};
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   COILED      417    444       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     266    266       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   448 AA;  51171 MW;  13EF7EE15AE0C0AB CRC64;
     MGLHSKKKVT DDFDFFEESL PKIEIPKNTQ DPMQVYQEIK DELMLDGNSK QNLATFCQTE
     VDDYIHRLMN DCIDKNMIDK DEYPQTAEIE SRCVNILANL WNATSDNTVG CSTTGSSEAA
     MLGGMAMKWR WRDKMKAQGK DYSKPNLITG PVQVCWHKFA RYWDIELREI PMSDESLIMT
     PEAVIERCDE NTIGVVPTLG VTFTGQYEPV EEVCKALDKF EKETGLDIPV HVDGASGGFL
     APFINPELKW DFRLPRVKSI NASGHKFGLS PLGVGWVVWT DKKYLPEDLV FNVNYLGGNM
     PTFALNFSRP GGQIVAQYFN FVRLGFEGYK KVHQISYDVT KYIAKKLKEL DRFEIIHDGD
     NGIPAVSWSL KKSKNYTLFD VSEKIRARGW QIAAYSMPKH REDLVVMRVL VRKGFTLDLA
     QLMLRDLKSV IDSLENKNDL KNKETFSH
//
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