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Database: UniProt/TrEMBL
Entry: A0A0E1N8W3_9GAMM
LinkDB: A0A0E1N8W3_9GAMM
Original site: A0A0E1N8W3_9GAMM 
ID   A0A0E1N8W3_9GAMM        Unreviewed;       446 AA.
AC   A0A0E1N8W3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   25-OCT-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=LA02_349 {ECO:0000313|EMBL:AJI57942.1};
OS   Francisella philomiragia.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=28110 {ECO:0000313|EMBL:AJI57942.1, ECO:0000313|Proteomes:UP000031885};
RN   [1] {ECO:0000313|EMBL:AJI57942.1, ECO:0000313|Proteomes:UP000031885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA01-2801 {ECO:0000313|EMBL:AJI57942.1,
RC   ECO:0000313|Proteomes:UP000031885};
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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP009444; AJI57942.1; -; Genomic_DNA.
DR   RefSeq; WP_042517023.1; NZ_CP009444.1.
DR   EnsemblBacteria; AJI57942; AJI57942; LA02_349.
DR   KEGG; fpj:LA02_349; -.
DR   KO; K01580; -.
DR   Proteomes; UP000031885; 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   Complete proteome {ECO:0000313|Proteomes:UP000031885};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AJI57942.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     264    264       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   446 AA;  50563 MW;  C07EB67A9F74D967 CRC64;
     MALHAKNDMK HKFYKESLPK FEIPKKSNDA FEAYQQIKDE LMLDGNSKQN LATFCQTEVD
     DFIHRLMDDC IDKNMIDKDE YPQTAEIESR CVNILANLWN SSAENAIGCS TTGSSEAAML
     GGMAMKWRWR DKMKAQGKDY TKPNLVTGPV QVCWHKFARY WDIELREIPM SSESLIMTPE
     TMLKYCDENT IGVVPTLGVT FTGQYEPVEA VCEALDKFER DTGIDIPVHV DAASGGFLAP
     FVEPELKWDF RLPRVKSINS SGHKFGLSPL GVGWVVWADK KYLPQDLIFN VNYLGGDMPT
     FALNFSRPGG QIVAQYYNFV KLGFEGYKNI HKLSYDVAKY IAKEIKDMGI FDIIHAGKGG
     IPAVSWSLKA GKSYDLFDIS EKIRARGWQI AAYSMPKDRQ DLVVMRVLVR RGFSFDLAEL
     MIRDLKNVIN SLDNKSKDIE RGGFSH
//
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