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Database: UniProt/TrEMBL
Entry: A0A0X8LMM9_VIBFL
LinkDB: A0A0X8LMM9_VIBFL
Original site: A0A0X8LMM9_VIBFL 
ID   A0A0X8LMM9_VIBFL        Unreviewed;       547 AA.
AC   A0A0X8LMM9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   07-JUN-2017, entry version 10.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:AMF94759.1};
GN   ORFNames=AL536_15020 {ECO:0000313|EMBL:AMF94759.1};
OS   Vibrio fluvialis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=676 {ECO:0000313|EMBL:AMF94759.1, ECO:0000313|Proteomes:UP000057088};
RN   [1] {ECO:0000313|EMBL:AMF94759.1, ECO:0000313|Proteomes:UP000057088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33809 {ECO:0000313|EMBL:AMF94759.1,
RC   ECO:0000313|Proteomes:UP000057088};
RA   Case J., Tallon L., Sadzewicz L., Sengamalay N., Ott S., Godinez A.,
RA   Nagaraj S., Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx
RT   tests.";
RL   Submitted (DEC-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; CP014035; AMF94759.1; -; Genomic_DNA.
DR   RefSeq; WP_020327717.1; NZ_CP014035.1.
DR   EnsemblBacteria; AMF94759; AMF94759; AL536_15020.
DR   GeneID; 29384694; -.
DR   KEGG; vfl:AL536_15020; -.
DR   KO; K01580; -.
DR   Proteomes; UP000057088; 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:UP000057088};
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;  61255 MW;  C839570650D9F624 CRC64;
     MVSEHKIADA NFETLLRIFT VPEGPDSTLT RIEEELSRNL NKFLREHIVA EEKPLKEIEK
     DFSDARIPDE PEFVSDHTQH LLDTLVAQSV HTASPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMLHRLIYGE QDSFYQQWMH SAEHSLGAFC SGGTIANITA
     LWVARNNALK ADGDFHGVEK EGLFKAMRHY GYEGLAILVS ERGHYSLKKA ADVLGIGQEG
     LVSVKTDENN RICPEDLKRK ITELKANNIK PFAVVGVAGT TETGNVDPLR IMAEISHQEG
     CHFHVDAAWG GATLMSNHHR HLLDGVELAD SVTIDAHKQL YIPMGAGMVL FKDPSAMNSI
     EHHAQYILRK GSKDLGSHTL EGSRSGMAML VYASMHIISR AGYELLIDQS IAKARYFADL
     IQAQDDFELV SQPELCLLTY RYLPSHIRQA LEKANADDQV LLNELLNELT KFIQKKQRET
     GKSFVSRTRL NPICWNKLDT IVFRVVLANP LTTNEILQSV LEEQRQIAAL APNLMGRIEH
     LAKQILA
//
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