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Database: UniProt/TrEMBL
Entry: B5FCJ1_VIBFM
LinkDB: B5FCJ1_VIBFM
Original site: B5FCJ1_VIBFM 
ID   B5FCJ1_VIBFM            Unreviewed;       547 AA.
AC   B5FCJ1;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:ACH65184.1};
GN   OrderedLocusNames=VFMJ11_0930 {ECO:0000313|EMBL:ACH65184.1};
OS   Vibrio fischeri (strain MJ11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=388396 {ECO:0000313|EMBL:ACH65184.1, ECO:0000313|Proteomes:UP000001857};
RN   [1] {ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|Proteomes:UP000001857};
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J.,
RA   Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R.,
RA   Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001139; ACH65184.1; -; Genomic_DNA.
DR   RefSeq; WP_012532876.1; NC_011184.1.
DR   ProteinModelPortal; B5FCJ1; -.
DR   EnsemblBacteria; ACH65184; ACH65184; VFMJ11_0930.
DR   KEGG; vfm:VFMJ11_0930; -.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; VFIS388396:G13HN-931-MONOMER; -.
DR   Proteomes; UP000001857; Chromosome I.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR022517; Asp_decarboxylase_pyridox.
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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03799; NOD_PanD_pyr; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001857};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   547 AA;  61011 MW;  69572E3FC7F7F31F CRC64;
     MVTDNKTADA SFESLLRIFT VPEAPDSTLG IIEKELSQNL NQFLREHIVA EEKPLTEIEK
     DFTDSSMPES PTYVSEHTEH LLDTLVSQSV HTSAPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMLHRLIFGQ KDSFYQHWMH SADHSLGAFC SGGTIANITA
     LWVARNRLLK PEGDFEGIAK QGLFAALTHY KCNGLAIFVS ERGHYSLKKA ADVLGIGQDG
     VIAVKTDNNN RVCLDDLELK ITQAKAKNIK PLAIVGVAGT TETGSIDPLR ELANVAQREG
     CHFHVDAAWG GATLMSNTYR HLLDGIDLAD SVTIDAHKQL YVPMGAGMVI FKDPELMSSI
     QHHAEYILRK GSKDLGRHTL EGSRSGMAML LYSCFNVISR PGYELLINQS IEKAHYFADL
     IQQQDDFELI TDPELCLLTY RYVPSNVKAA LAIATDEQKL EIYEHLDNLT KYIQKTQRET
     GKSFVSRTRL TPEAYQHQPT IVFRVVLANP LTTKEILQNV LIEQREIASS SEISLPLLNQ
     IVDKILH
//
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