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Database: UniProt/TrEMBL
Entry: A0A1S6HNK9_9GAMM
LinkDB: A0A1S6HNK9_9GAMM
Original site: A0A1S6HNK9_9GAMM 
ID   A0A1S6HNK9_9GAMM        Unreviewed;       550 AA.
AC   A0A1S6HNK9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   23-MAY-2018, entry version 7.
DE   SubName: Full=Putative pyridoxal-dependent aspartate 1-decarboxylase {ECO:0000313|EMBL:AQS37098.1};
DE            EC=4.1.1.15 {ECO:0000313|EMBL:AQS37098.1};
GN   ORFNames=Sps_01938 {ECO:0000313|EMBL:AQS37098.1};
OS   Shewanella psychrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225848 {ECO:0000313|EMBL:AQS37098.1, ECO:0000313|Proteomes:UP000189545};
RN   [1] {ECO:0000313|EMBL:AQS37098.1, ECO:0000313|Proteomes:UP000189545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP2 {ECO:0000313|EMBL:AQS37098.1,
RC   ECO:0000313|Proteomes:UP000189545};
RA   Xu G., Jian H.;
RT   "Complete genome sequence of Shewanella psychrophila WP2, a deep sea
RT   bacterium isolated from west Pacific sediment.";
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; CP014782; AQS37098.1; -; Genomic_DNA.
DR   KEGG; spsw:Sps_01938; -.
DR   KO; K01580; -.
DR   Proteomes; UP000189545; Chromosome.
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   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.
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:UP000189545};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:AQS37098.1};
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   550 AA;  61060 MW;  BF2468231540EF6C CRC64;
     MSMTPRRATA SEEALLRIFT VPEAPDSTLS VIEQNISQNL MGFLQESVVA IEKPLSEIEL
     DFQQHQIPSA PQFVSDYADD MMKTLVAHSV HTSSPSFIGH MTSALPYFVL PLSKMMVGLN
     QNLVKIETSK AFTPLERQVL GMMHHLIYSE DDKFYKSWMH SANYSLGAFC SGGTVANITA
     LWTARNQLLK ADGDFKGVSA QGLMKGLRHY GYDDLAILVS ERGHYSLAKT ADLLGIGREN
     IIQIPTSNDN KVDVDKMRAM AKQLEHDNIK VMAIVGVAGT TETGNIDPLD ELATLASELK
     CHFHVDAAWG GASLLSNKYR HLLKGIERAD SVTIDAHKQM YVPMGAGMVI FKDPAFANAI
     KHHAEYILRK GSKDLGSQTL EGSRPGMAML VHACLQVIGR DGYEILINNS LEKARYFAEL
     IQDHSDFQLV SEPELCLLTY RYVPKQVQVA MLQARESGNA DKLIEFNRVL DGLTKFVQKR
     QREQGTSFVS RTRINPESEI GLNIKSVVFR VVLANPLTTH EILQQVLAEQ IEIASQDDNF
     LPQLLALASE
//
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