GenomeNet

Database: UniProt
Entry: B7LE63
LinkDB: B7LE63
Original site: B7LE63 
ID   MGSA_ECO55              Reviewed;         152 AA.
AC   B7LE63;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   19-FEB-2014, entry version 30.
DE   RecName: Full=Methylglyoxal synthase;
DE            Short=MGS;
DE            EC=4.2.3.3;
GN   Name=mgsA; OrderedLocusNames=EC55989_1012;
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- CATALYTIC ACTIVITY: Glycerone phosphate = methylglyoxal +
CC       phosphate.
CC   -!- SIMILARITY: Belongs to the methylglyoxal synthase family.
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DR   EMBL; CU928145; CAU96874.1; -; Genomic_DNA.
DR   RefSeq; YP_002402105.1; NC_011748.1.
DR   ProteinModelPortal; B7LE63; -.
DR   SMR; B7LE63; 1-151.
DR   STRING; 585055.EC55989_1012; -.
DR   EnsemblBacteria; CAU96874; CAU96874; EC55989_1012.
DR   GeneID; 7146406; -.
DR   KEGG; eck:EC55989_1012; -.
DR   PATRIC; 38475429; VBIEscCol113220_1031.
DR   eggNOG; COG1803; -.
DR   HOGENOM; HOG000283729; -.
DR   KO; K01734; -.
DR   OMA; EPQPHDP; -.
DR   OrthoDB; EOG644ZN1; -.
DR   ProtClustDB; PRK05234; -.
DR   BioCyc; ECOL585055:GJOM-1030-MONOMER; -.
DR   GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019242; P:methylglyoxal biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   HAMAP; MF_00549; Methylglyoxal_synth; 1.
DR   InterPro; IPR004363; Methylgl_synth.
DR   InterPro; IPR018148; Methylglyoxal_synth_AS.
DR   InterPro; IPR011607; MGS-like_dom.
DR   Pfam; PF02142; MGS; 1.
DR   PIRSF; PIRSF006614; Methylglyox_syn; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   TIGRFAMs; TIGR00160; MGSA; 1.
DR   PROSITE; PS01335; METHYLGLYOXAL_SYNTH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Lyase.
FT   CHAIN         1    152       Methylglyoxal synthase.
FT                                /FTId=PRO_1000146625.
FT   ACT_SITE     71     71       By similarity.
SQ   SEQUENCE   152 AA;  16933 MW;  0E96DA03A3A3F9DC CRC64;
     MELTTRTLPA RKHIALVAHD HCKQMLMSWV ERHQPLLEQH VLYATGTTGN LISRATGMNI
     NAMLSGPMGG DQQVGALISE GKIDVLIFFW DPLNAVPHDP DVKALLRLAT VWNIPVATNV
     ATADFIIQSP HFNDAVDILI PDYQRYLADR LK
//
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