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Database: UniProt/TrEMBL
Entry: A0A0C5WRF6_9GAMM
LinkDB: A0A0C5WRF6_9GAMM
Original site: A0A0C5WRF6_9GAMM 
ID   A0A0C5WRF6_9GAMM        Unreviewed;       553 AA.
AC   A0A0C5WRF6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   07-JUN-2017, entry version 9.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:AJR08932.1};
GN   ORFNames=H744_2c2269 {ECO:0000313|EMBL:AJR08932.1};
OS   Photobacterium gaetbulicola Gung47.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR08932.1, ECO:0000313|Proteomes:UP000032303};
RN   [1] {ECO:0000313|EMBL:AJR08932.1, ECO:0000313|Proteomes:UP000032303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gung47 {ECO:0000313|EMBL:AJR08932.1,
RC   ECO:0000313|Proteomes:UP000032303};
RA   Kim Y.-O.;
RT   "Complete genome sequence of the lipase-producing bacterium
RT   Photobacterium gaetbulicola Gung47.";
RL   Submitted (MAY-2013) 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; CP005974; AJR08932.1; -; Genomic_DNA.
DR   RefSeq; WP_044623529.1; NZ_CP005974.1.
DR   EnsemblBacteria; AJR08932; AJR08932; H744_2c2269.
DR   KEGG; pgb:H744_2c2269; -.
DR   PATRIC; fig|658445.3.peg.4261; -.
DR   KO; K01580; -.
DR   Proteomes; UP000032303; 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:UP000032303};
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:UP000032303}.
FT   MOD_RES     339    339       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   553 AA;  61707 MW;  F91E8BF31DA73B1B CRC64;
     MAVVDHKKAD ATQESLHRIF TVPEAPESTL GRIEKEISEN LNVFLQTHIA AREKPLAEIE
     KDFSSADIPE SPSFVSDHTH FLLDKLVAQS VHTSAPTFIG HMTSALPYFL MPLSKIMIGL
     NQNLVKIETS KAFTPLERQV LGMLHNLIYR ENDAFYQQWM HSANHSLGAF CSGGTIANIT
     ALWVARNSAL KPDGDFKGVA QEGLFKAMKH YGYEDLVVLV SERGHYSLKK AADVLGLGRD
     CLIPIKTDGH NRVRVDDMRA KLEELKQNQV KAFAIVGVAG TTETGNIDPL EELADLAQEY
     GCHFHVDAAW GGATLMSNTY RPLLKGIERA DSVTIDAHKQ LYVPMGAGMV IFKNPALMTA
     IEHHAEYILR KGSKDLGSHT LEGSRSGMAM LLYASLNIIS RPGYEMLINT SIEKAQYFAS
     LINQDSDFEL ISEPELCLLT YRYAPARTQE ALKLADPEQR EELLAALDDM TKFIQKRQRE
     SGKSFVSRTR ITPQAWGRRL TTVFRVVLAN PLTTEQILKD VLEEQKDIAK QSLISFPKIN
     TLTESILNQQ VTL
//
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