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Database: UniProt/TrEMBL
Entry: C6YTR0_9GAMM
LinkDB: C6YTR0_9GAMM
Original site: C6YTR0_9GAMM 
ID   C6YTR0_9GAMM            Unreviewed;       446 AA.
AC   C6YTR0;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   05-JUL-2017, entry version 42.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=BZ13_1128 {ECO:0000313|EMBL:AJI74183.1};
OS   Francisella philomiragia subsp. philomiragia ATCC 25015.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=539329 {ECO:0000313|EMBL:AJI74183.1, ECO:0000313|Proteomes:UP000031897};
RN   [1] {ECO:0000313|EMBL:AJI74183.1, ECO:0000313|Proteomes:UP000031897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O#319L {ECO:0000313|EMBL:AJI74183.1};
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; CP010019; AJI74183.1; -; Genomic_DNA.
DR   RefSeq; WP_004286925.1; NZ_DS999312.1.
DR   EnsemblBacteria; AJI74183; AJI74183; BZ13_1128.
DR   KEGG; fpt:BZ13_1128; -.
DR   PATRIC; fig|539329.6.peg.1110; -.
DR   KO; K01580; -.
DR   Proteomes; UP000031897; 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:UP000031897};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:AJI74183.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     264    264       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   446 AA;  50495 MW;  F0B2F43AAFF4A6A9 CRC64;
     MALHAKNNIK HKLYKESLPK FEIPKKSNDA FEAYQQIKDE LMLDGNSKQN LATFCQTEVD
     DFIHKLMDDC IDKNMIDKDE YPQTAEIESR CVNILANLWN SSAENAIGCS TTGSSEAAML
     GGMAMKWRWR DKMKAQGKDY TKPNLVTGPV QVCWHKFARY WDIELREIPM SSESLIMTPE
     TMLKYCDENT IGVVPTLGVT FTGQYEPVEA VCEALDKFER ETGINIPVHV 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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