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Database: UniProt/TrEMBL
Entry: Q87QB3_VIBPA
LinkDB: Q87QB3_VIBPA
Original site: Q87QB3_VIBPA 
ID   Q87QB3_VIBPA            Unreviewed;       548 AA.
AC   Q87QB3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   07-JUN-2017, entry version 78.
DE   SubName: Full=Putative glutamate decarboxylase {ECO:0000313|EMBL:BAC59500.1};
GN   OrderedLocusNames=VP1237 {ECO:0000313|EMBL:BAC59500.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59500.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC59500.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC59500.1; -; Genomic_DNA.
DR   RefSeq; NP_797616.1; NC_004603.1.
DR   RefSeq; WP_005483514.1; NC_004603.1.
DR   ProteinModelPortal; Q87QB3; -.
DR   STRING; 223926.VP1237; -.
DR   DNASU; 1188742; -.
DR   EnsemblBacteria; BAC59500; BAC59500; BAC59500.
DR   GeneID; 1188742; -.
DR   KEGG; vpa:VP1237; -.
DR   PATRIC; fig|223926.6.peg.1176; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   BioCyc; VPAR223926:GHK4-1285-MONOMER; -.
DR   Proteomes; UP000002493; 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   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:UP000002493};
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:UP000002493}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   548 AA;  61268 MW;  CD0473BE69A9EE06 CRC64;
     MVKEQKTADV SFESLLKIFT VPEGPDSTLT KIDESLSRNL NQFLREHIVA EEKPLREIEK
     DFSSAQIPEQ PEFVSDHTEH LLDTLVSHSV HTSAPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMLHRLIYGQ NDKFYRKWMH SANHSLGAFC SGGTIANITA
     LWVARNKALK ADGAFNGVEK EGLFKAMKHY GYEGLAVLVS ERGHYSLKKA ADVLGLGQEG
     LVAVKTDANN RIVVDDLKTK IAELKEQNIK PIAVIGVAGT TETGSVDPLS QIAQVCQEHN
     CHFHVDAAWG GATLMSNHYR HLLEGVELAD SVTIDAHKQL YIPMGAGMVL FKDPDAMKSI
     EHHAQYILRK GSKDLGSHTL EGSRSGMAML VYAAMHIISR PGYELLIDQS IEKARYFADL
     IKQQDDFELV SEPELCLLTY RYLPPLIREA LDKAEGTQKE KLNELINQLT QFIQKRQRET
     GKSFVSRTRL NPDQWQRMNT IVFRVVLANP LTTRDILSSV LDEQREIAKQ APSLTAKIEE
     MASDILGA
//
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