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Database: UniProt/TrEMBL
Entry: G0ASU8_9GAMM
LinkDB: G0ASU8_9GAMM
Original site: G0ASU8_9GAMM 
ID   G0ASU8_9GAMM            Unreviewed;       549 AA.
AC   G0ASU8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   28-FEB-2018, entry version 29.
DE   SubName: Full=Putative pyridoxal-dependent aspartate 1-decarboxylase {ECO:0000313|EMBL:AEG12003.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:AEG12003.1};
GN   ORFNames=Sbal175_2759 {ECO:0000313|EMBL:AEG12003.1};
OS   Shewanella baltica BA175.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG12003.1, ECO:0000313|Proteomes:UP000002249};
RN   [1] {ECO:0000313|EMBL:AEG12003.1, ECO:0000313|Proteomes:UP000002249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA175 {ECO:0000313|EMBL:AEG12003.1,
RC   ECO:0000313|Proteomes:UP000002249};
RX   PubMed=22328742; DOI=10.1128/JB.06468-11;
RA   Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M.,
RA   Tiedje J.M., Konstantinidis K.T.;
RT   "Genome sequencing of five Shewanella baltica strains recovered from
RT   the oxic-anoxic interface of the Baltic Sea.";
RL   J. Bacteriol. 194:1236-1236(2012).
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; CP002767; AEG12003.1; -; Genomic_DNA.
DR   RefSeq; WP_006081099.1; NC_017571.1.
DR   EnsemblBacteria; AEG12003; AEG12003; Sbal175_2759.
DR   KEGG; sbb:Sbal175_2759; -.
DR   KO; K01580; -.
DR   Proteomes; UP000002249; Chromosome.
DR   GO; GO:0033983; F:diaminobutyrate 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:UP000002249};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:AEG12003.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     339    339       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   549 AA;  60672 MW;  AB7BC4038820D4D0 CRC64;
     MTQKLPRQAT ASEESLLRIF TAPEDAGSTL SIIEQKLSED LAGFLGDSIA ALEKPLSEIE
     TDFQAFEIPT QPRFVSDYTD EIMQNLVAHS VHTAAPSFIG HMTSALPYFV LPLSKMMVGL
     NQNLVKIETS KAFTPLERQV LGMMHHLIYD QDTDFYQSWM HSANHSLGAF CSGGTVANIT
     ALWIARNQLL KADGEFKGVS REGLLKALRH YGYDDLAILV SERGHYSLGK AVDLLGIGRD
     NIISIPTGRD NKVDVAKMRQ AALELASKNI KVLAIVGVAG TTETGNVDPL TELAALAKEL
     NCHFHVDAAW GGASLLSNKY RHLLAGIELA DSVTIDAHKQ MYVPMGAGMV LFKDPEFAHA
     IAHHAEYILR RGSKDLGSQT LEGSRPGMAM LVHACLQIIG RDGYEILINN SLEKARYFAE
     QIKAHEDFEL VTEPELCLLT YRYVPACVQA AMQLACEQAD TLRLARFNEL LDGLTQFIQK
     HQREQGKSFV SRTRIQPARY FRQATVVFRV VLANPLTSHD ILNQVLIEQS EIAALDNEFL
     PALLAMVAE
//
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