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Database: UniProt/TrEMBL
Entry: A0A0H6KPP7_VIBCL
LinkDB: A0A0H6KPP7_VIBCL
Original site: A0A0H6KPP7_VIBCL 
ID   A0A0H6KPP7_VIBCL        Unreviewed;       548 AA.
AC   A0A0H6KPP7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   05-JUL-2017, entry version 13.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:CSB53059.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:CSB53059.1};
GN   Name=ddc_1 {ECO:0000313|EMBL:CSB53059.1};
GN   ORFNames=ERS013201_00153 {ECO:0000313|EMBL:CSB53059.1};
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=666 {ECO:0000313|EMBL:CSB53059.1, ECO:0000313|Proteomes:UP000046067};
RN   [1] {ECO:0000313|EMBL:CSB53059.1, ECO:0000313|Proteomes:UP000046067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A325 {ECO:0000313|EMBL:CSB53059.1,
RC   ECO:0000313|Proteomes:UP000046067};
RA   Informatics Pathogen;
RL   Submitted (JUL-2015) 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; CWQJ01000001; CSB53059.1; -; Genomic_DNA.
DR   RefSeq; WP_000253198.1; NZ_MOLM01000005.1.
DR   EnsemblBacteria; CSB53059; CSB53059; ERS013201_00153.
DR   EnsemblBacteria; OEC21723; OEC21723; BFX10_05705.
DR   KEGG; vcx:VAA049_2590; -.
DR   PATRIC; fig|666.1974.peg.816; -.
DR   KO; K01580; -.
DR   Proteomes; UP000046067; Unassembled WGS sequence.
DR   GO; GO:0033983; F:diaminobutyrate decarboxylase activity; IEA:UniProtKB-EC.
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:UP000046067};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:CSB53059.1};
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;  61609 MW;  ED7788009B600B58 CRC64;
     MVSEHKSAQV NFDSLLKIFT VPEGPDSTLT KIDEELSRNL NHFLRKHIVA EEKPLKEIEK
     DFSNAHIPEQ PQFVSDHTQH 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 RYLPAHVRMA LEKSQGVQRA QLNELLNELT KFIQKKQRET
     GKSFVSRTQL NPHQWDKLAT IVFRVVLANP LTTKEILHNV LDEQREIAQQ APKLMRQIEH
     LTQCILNQ
//
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