GenomeNet

Database: UniProt/TrEMBL
Entry: B7VPR7_VIBTL
LinkDB: B7VPR7_VIBTL
Original site: B7VPR7_VIBTL 
ID   B7VPR7_VIBTL            Unreviewed;       547 AA.
AC   B7VPR7;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   28-MAR-2018, entry version 52.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:CAV19017.1};
GN   OrderedLocusNames=VS_1833 {ECO:0000313|EMBL:CAV19017.1};
OS   Vibrio tasmaniensis (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=575788 {ECO:0000313|EMBL:CAV19017.1, ECO:0000313|Proteomes:UP000009100};
RN   [1] {ECO:0000313|EMBL:CAV19017.1, ECO:0000313|Proteomes:UP000009100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32 {ECO:0000313|EMBL:CAV19017.1,
RC   ECO:0000313|Proteomes:UP000009100};
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; FM954972; CAV19017.1; -; Genomic_DNA.
DR   RefSeq; WP_012604236.1; NC_011753.2.
DR   STRING; 575788.VS_1833; -.
DR   EnsemblBacteria; CAV19017; CAV19017; VS_1833.
DR   GeneID; 7161397; -.
DR   KEGG; vsp:VS_1833; -.
DR   PATRIC; fig|575788.5.peg.3124; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; FHKHFFQ; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; VSPL575788:GH64-1800-MONOMER; -.
DR   Proteomes; UP000009100; Chromosome 1.
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   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.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03799; NOD_PanD_pyr; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009100};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009100}.
FT   COILED      459    479       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   547 AA;  61243 MW;  A7C4ED128CA971C7 CRC64;
     MVTEQKTADV SFDSLLRIFT VPEGPDSTLT QIEDKLSRNL NQFLREHIVA EEKPLREIEK
     DFSNAHIPEQ PEFVSEHTEH LLDSLVSHSV HTSSPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMLHRLIYQD SDQFYSRWMH SANHSLGAFC SGGTIANITA
     LWVARNNALK AQGSFKGVEK EGLFKAMKHY GYEGLAILVS ERGHYSLKKA ADVLGIGQEG
     LVSVKTDNDN RICTDDLRLK IEQLKQNKIK PFAVIGVAGT TETGNIDPLR DIAEVCAESD
     CHFHVDAAWG GATLMSNNHR HLLDGIELAD SVTIDAHKQL YIPMGAGMVL FKKPDAMTAI
     EHHAQYILRK GSKDLGSHTL EGSRSGMAML VYASMHIISR PGYELLIDQS INKARYFADL
     IKNQNDFELV SEPELCLLTY RYVPESVKAA LLKAKAPERV ELNELLNELT KFIQKKQRET
     GKSFVSRTRL NPEIWAHQPI IVFRVVLANP LTGKDILSSV LEEQREISKL APNLMSKITK
     LVKLINA
//
DBGET integrated database retrieval system