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Database: UniProt/TrEMBL
Entry: A0A0H3AK76_VIBC3
LinkDB: A0A0H3AK76_VIBC3
Original site: A0A0H3AK76_VIBC3 
ID   A0A0H3AK76_VIBC3        Unreviewed;       548 AA.
AC   A0A0H3AK76;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 11.
DE   SubName: Full=Putative glutamate decarboxylase {ECO:0000313|EMBL:ABQ20604.1};
GN   OrderedLocusNames=VC0395_A0719 {ECO:0000313|EMBL:ABQ20604.1};
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=345073 {ECO:0000313|EMBL:ABQ20604.1, ECO:0000313|Proteomes:UP000000249};
RN   [1] {ECO:0000313|EMBL:ABQ20604.1, ECO:0000313|Proteomes:UP000000249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395
RC   {ECO:0000313|Proteomes:UP000000249};
RA   Heidelberg J.;
RL   Submitted (MAR-2007) 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; CP000627; ABQ20604.1; -; Genomic_DNA.
DR   RefSeq; WP_000253201.1; NC_012582.1.
DR   ProteinModelPortal; A0A0H3AK76; -.
DR   STRING; 345073.VC0395_A0719; -.
DR   EnsemblBacteria; ABQ20604; ABQ20604; VC0395_A0719.
DR   KEGG; vco:VC0395_A0719; -.
DR   PATRIC; fig|345073.21.peg.1183; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   Proteomes; UP000000249; Chromosome 2.
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:UP000000249};
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   548 AA;  61693 MW;  DCBFD48556AF50B2 CRC64;
     MVSEHKSAQV NFDSLLKIFT VPEGPDSTLT KIDEELSRNL NHFLRKHIVA EEKPLKEIEK
     DFSNAHIPEQ PQFVSDHTQY LLDTLVSHSV HTASPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMIHRLIYGE TDHFYQQWMH SAEHSLGAFC SGGTIANITA
     LWVARNNALK AEGDFPGVEK AGLFKAMRHY GHEGLAILVS ERGHYSLKKA ADVLGIGQEG
     LVAVKTDAHN RICPHDLEQK ITELKANKIK VFAVVGVAGT TETGNIDPLR TIAQICQREQ
     IHFHIDAAWG GATLMSNRYR GLLDGVELAD SVTIDAHKQL YIPMGAGMVL FKDPNAMRSI
     EHHAQYILRQ GSKDLGSHTL EGSRSGMAML VYASMHIISR PGYQLLIDQS IEKARYFADL
     IDAQTDFELV SQPELCLLTY RYLPEHVRMA LEKSQGVQRA QLNELLNELT KFIQKKQRET
     GKSFVSRTQL NPHQWDKLAT IVFRVVLANP LTTKEILHNV LDEQREIAQQ APKLMRQIEH
     LTQCILNQ
//
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