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Database: UniProt/TrEMBL
Entry: A0A1B1NNJ2_9VIBR
LinkDB: A0A1B1NNJ2_9VIBR
Original site: A0A1B1NNJ2_9VIBR 
ID   A0A1B1NNJ2_9VIBR        Unreviewed;       540 AA.
AC   A0A1B1NNJ2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   07-JUN-2017, entry version 6.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:ANS85317.1};
DE            EC=4.1.1.15 {ECO:0000313|EMBL:ANS85317.1};
GN   Name=gadB {ECO:0000313|EMBL:ANS85317.1};
GN   ORFNames=VSVS05_01172 {ECO:0000313|EMBL:ANU36299.1}, VSVS12_01550
GN   {ECO:0000313|EMBL:ANS85317.1};
OS   Vibrio scophthalmi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=45658 {ECO:0000313|EMBL:ANS85317.1, ECO:0000313|Proteomes:UP000092656};
RN   [1] {ECO:0000313|EMBL:ANS85317.1, ECO:0000313|Proteomes:UP000092656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VS-12 {ECO:0000313|EMBL:ANS85317.1,
RC   ECO:0000313|Proteomes:UP000092656};
RA   Han H.-J.;
RT   "Genome sequencing of Vibrio scophthalmi strain VS-12, an isolated
RT   from Paralichthys olivaceus.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANU36299.1, ECO:0000313|Proteomes:UP000092528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VS-05 {ECO:0000313|EMBL:ANU36299.1,
RC   ECO:0000313|Proteomes:UP000092528};
RA   Han H.-J.;
RT   "Genome sequencing of Vibrio scophthalmi strain VS-05, an isolated
RT   from Paralichthys olivaceus.";
RL   Submitted (JUL-2016) 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; CP016307; ANS85317.1; -; Genomic_DNA.
DR   EMBL; CP016414; ANU36299.1; -; Genomic_DNA.
DR   EnsemblBacteria; ANS85317; ANS85317; VSVS12_01550.
DR   EnsemblBacteria; ANU36299; ANU36299; VSVS05_01172.
DR   KEGG; vsc:VSVS12_01550; -.
DR   PATRIC; fig|45658.6.peg.1507; -.
DR   KO; K01580; -.
DR   Proteomes; UP000092528; Chromosome 1.
DR   Proteomes; UP000092656; Chromosome 1.
DR   GO; GO:0004351; F:glutamate 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:UP000092528,
KW   ECO:0000313|Proteomes:UP000092656};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:ANS85317.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     332    332       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   540 AA;  60479 MW;  F0E5348B0382F4AD CRC64;
     MADVSFESLL RIFTVPEGPD STLTQIEEEL SRNLNKFLRE HIVAEEKPLR EIEKDFSCAV
     IPEQPEFVSE HTQHLLDTLV SHSVHTSAPS FIGHMTSALP YFLMPLSKIM IALNQNLVKI
     ETSKAFTPLE RQVLGMLHRL IYSQDHGFYQ QWMHSANHSL GAFCSGGTIA NITALWVARN
     NALRAQGHFR GVEKEGLFKA MKHYGYEGLA ILVSERGHYS LKKAADVLGI GQDGLVAVKT
     DSNNRICPDD LKLKIKELKD KKIKPFAVIG VAGTTETGNI DPLKAMAAIC QAEGCHFHVD
     AAWGGATLMS NRYRHLLDGI ELADSVTIDA HKQLYIPMGA GMVLFKDPSS MKSIEHHAQY
     ILRKGSKDLG SHTLEGSRSG MAMLVYAAMH IISRPGYELL INQSIEKARY FADLIEQQAD
     FELVSQPELC LLTYRYLPRH VREALEKANP AQRTELNGLL NELTKFVQKR QRENGRSFVS
     RTRLNPVHWD DLNTIVFRVV LANPLTTCDI LQSVLEEQRE IALHGAPSLL EKIESLASKL
//
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