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Database: UniProt/TrEMBL
Entry: A0A1D8RWI4_9GAMM
LinkDB: A0A1D8RWI4_9GAMM
Original site: A0A1D8RWI4_9GAMM 
ID   A0A1D8RWI4_9GAMM        Unreviewed;       542 AA.
AC   A0A1D8RWI4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-SEP-2017, entry version 6.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:AOW77458.1};
GN   ORFNames=A3Q34_11665 {ECO:0000313|EMBL:AOW77458.1};
OS   Colwellia sp. PAMC 20917.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=1816218 {ECO:0000313|EMBL:AOW77458.1, ECO:0000313|Proteomes:UP000177820};
RN   [1] {ECO:0000313|EMBL:AOW77458.1, ECO:0000313|Proteomes:UP000177820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 20917 {ECO:0000313|EMBL:AOW77458.1,
RC   ECO:0000313|Proteomes:UP000177820};
RA   Kim H.-W.;
RT   "Complete genome sequence of Colwellia sp. PAMC 20917.";
RL   Submitted (MAR-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; CP014944; AOW77458.1; -; Genomic_DNA.
DR   RefSeq; WP_070375524.1; NZ_CP014944.1.
DR   KEGG; coz:A3Q34_11665; -.
DR   KO; K01580; -.
DR   Proteomes; UP000177820; Chromosome.
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:UP000177820};
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:UP000177820}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   542 AA;  60535 MW;  2194E715FA07AA83 CRC64;
     MTTNKRTAKA TQESLHSIFT IPEAPDSTLG LIEKEISENL AGFLGNHIAA KERALSEIEK
     DFASSAIPEE PSFVSDHTRH ILDKVVAQSV HTSSPSFIGH MTSALPYFIL PLSKLMVGLN
     QNLVKIETSK AFTPLERQVL GMMHRLVYKD NDHFYEQWMH SANHSLGAFC SGGTVANLTA
     FWVARNNLLK ADGDFKGIAR EGLFNALKHY KYDGLVILVS DRGHYSLKKS ADILGIGQDS
     VISIPTDGHN RIDCQKLREK CLELKQRNIR VLSIVGVAGT TETGNIDPLD KMADIAEEFQ
     THFHVDAAWG GATLLSNKYR PLLKGIERAD SVTIDAHKQM YVPMGAGLVV FKNPASVASI
     EHHAEYILRK GSKDLGSHTL EGSRPGMAML VYASLHIISR PGYEMLINQG IDRARYFAER
     INQHADFELI TEPELCLLTY RYNPKAVQNL LANSSAEQQD KINDLLDDLT KFIQKRQREN
     GKSFVSRTRI EVQRYQGRKT VVFRVVLANP LTSNEILNDV LVEQLELAQE SETFLPDLLS
     LT
//
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