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Database: UniProt/TrEMBL
Entry: A0Q8J3_FRATN
LinkDB: A0Q8J3_FRATN
Original site: A0Q8J3_FRATN 
ID   A0Q8J3_FRATN            Unreviewed;       448 AA.
AC   A0Q8J3;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   05-JUL-2017, entry version 68.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=FTN_1701 {ECO:0000313|EMBL:ABK90558.1};
OS   Francisella tularensis subsp. novicida (strain U112).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=401614 {ECO:0000313|EMBL:ABK90558.1, ECO:0000313|Proteomes:UP000000762};
RN   [1] {ECO:0000313|Proteomes:UP000000762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U112 {ECO:0000313|Proteomes:UP000000762};
RX   PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA   Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J.,
RA   Radey M., Guina T., Svensson K., Hayden H.S., Jacobs M.,
RA   Gallagher L.A., Manoil C., Ernst R.K., Drees B., Buckley D.,
RA   Haugen E., Bovee D., Zhou Y., Chang J., Levy R., Lim R., Gillett W.,
RA   Guenthener D., Kang A., Shaffer S.A., Taylor G., Chen J., Gallis B.,
RA   D'Argenio D.A., Forsman M., Olson M.V., Goodlett D.R., Kaul R.,
RA   Miller S.I., Brittnacher M.J.;
RT   "Comparison of Francisella tularensis genomes reveals evolutionary
RT   events associated with the emergence of human pathogenic strains.";
RL   Genome Biol. 8:R102.1-R102.16(2007).
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; CP000439; ABK90558.1; -; Genomic_DNA.
DR   RefSeq; WP_003041366.1; NZ_CP009633.1.
DR   ProteinModelPortal; A0Q8J3; -.
DR   EnsemblBacteria; ABK90558; ABK90558; FTN_1701.
DR   KEGG; ftn:FTN_1701; -.
DR   KEGG; ftx:AW25_287; -.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; DSCGCVT; -.
DR   BioCyc; FTUL401614:G12WZ-1689-MONOMER; -.
DR   Proteomes; UP000000762; 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:UP000000762};
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   448 AA;  50828 MW;  B5798B19FE0FA0D4 CRC64;
     MALHGKKDTI NNLDFFEQSL PKFKLPLNSQ DPLEVYQEIK DELMLDGNSK QNLATFCQTE
     VDDFIHKLMD DCIDKNMIDK DEYPQTAEIE SRCVNILANL WNSSAENAIG CSTTGSSEAA
     MLGGMAMKWR WRDKMKAQGK DYTKPNLVTG PVQVCWHKFA RYWDIELREI PMSNESLIMT
     PEAVLERCDE NTIGVVPTLG VTFTGQYEPV EQVCKALDDF ERQTGIDIPV HVDAASGGFL
     APFVEPELKW DFRLPRVKSI NSSGHKFGLS PLGVGWVIWA DKKYLPDDLI FNVNYLGGNM
     PTFALNFSRP GGQIVAQYYN FVRLGFEGYK KVHQLCYDVA EYIAKELRKM EIFEIIHAGE
     GGIPAVSWSL KATKEYSLFD ISEKVRAKGW QIAAYTMPTN REDLVVMRVL VRRGFSYDLA
     QLMIRDLVAV INSLEGKLKI LKRSSFAH
//
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