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Database: UniProt/TrEMBL
Entry: A0A0B6D402_9GAMM
LinkDB: A0A0B6D402_9GAMM
Original site: A0A0B6D402_9GAMM 
ID   A0A0B6D402_9GAMM        Unreviewed;       446 AA.
AC   A0A0B6D402;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUL-2017, entry version 19.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=LA55_1994 {ECO:0000313|EMBL:AJI53611.1};
OS   Francisella philomiragia.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=28110 {ECO:0000313|EMBL:AJI53611.1, ECO:0000313|Proteomes:UP000031830};
RN   [1] {ECO:0000313|EMBL:AJI53611.1, ECO:0000313|Proteomes:UP000031830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA01-2794 {ECO:0000313|EMBL:AJI53611.1,
RC   ECO:0000313|Proteomes:UP000031830};
RX   PubMed=25931589;
RA   Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G.,
RA   Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C.,
RA   Chertkov O., Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N.,
RA   Gibbons H.S., Palacios G.F., Redden C.L., Xu Y., Minogue T.D.,
RA   Chain P.S.;
RT   "Genome sequencing of 18 francisella strains to aid in assay
RT   development and testing.";
RL   Genome Announc. 3:0-0(2015).
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; CP009440; AJI53611.1; -; Genomic_DNA.
DR   RefSeq; WP_044526994.1; NZ_CP009440.1.
DR   EnsemblBacteria; AJI53611; AJI53611; LA55_1994.
DR   KEGG; fpz:LA55_1994; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   Proteomes; UP000031830; 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:UP000031830};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:AJI53611.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   COILED      415    442       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     264    264       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   446 AA;  50548 MW;  3D617781D8097874 CRC64;
     MALHAKNNIK HKLYKESLPK FEIPKKSNDA FEAYQQIKDE LMLDGNSKQN LATFCQTEVD
     DFIHKLMDDC IDKNMIDKDE YPQTAEIESR CVNILANLWN SSAESAIGCS TTGSSEAAML
     GGMAMKWRWR DKMKAQGKDY TKPNLVTGPV QVCWHKFARY WDIELREIPM SNESLIMTPE
     TMLKYCDENT IGVVPTLGVT FTGQYEPVEA VCEALDKFER DTGIDIPVHV DAASGGFLAP
     FVEPELKWDF RLPRVKSINS SGHKFGLSPL GVGWVVWADK KYLPQDLIFN VNYLGGDMPT
     FALNFSRPGG QIVAQYYNFV KLGFEGYKNI HKLSYDVAKY IAKEIKDMGI FDIIHAGKGG
     IPAVSWSLKA GKSYDLFDIS EKIRARGWQI AAYSMPKDRQ DLVVMRVLVR RGFSFDLAEL
     MIRDLKNVID SLEHKSRDIE RGGFSH
//
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