ID MGSA_BRUSU Reviewed; 125 AA.
AC P0A3Q3; G0KE54; Q44615;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 01-MAY-2013, entry version 49.
DE RecName: Full=Methylglyoxal synthase;
DE Short=MGS;
DE EC=4.2.3.3;
GN Name=mgsA; OrderedLocusNames=BRA1048, BS1330_II1040;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Brucellaceae; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between
RT animal and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/JB.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- CATALYTIC ACTIVITY: Glycerone phosphate = methylglyoxal +
CC phosphate.
CC -!- SIMILARITY: Belongs to the methylglyoxal synthase family.
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DR EMBL; AE014292; AAN34215.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM20492.1; -; Genomic_DNA.
DR RefSeq; NP_700210.1; NC_004311.2.
DR RefSeq; YP_005614718.1; NC_017250.1.
DR ProteinModelPortal; P0A3Q3; -.
DR SMR; P0A3Q3; 1-124.
DR STRING; 204722.BRA1048; -.
DR EnsemblBacteria; AAN34215; AAN34215; BRA1048.
DR EnsemblBacteria; AEM20492; AEM20492; BS1330_II1040.
DR GeneID; 1165493; -.
DR GeneID; 12139273; -.
DR KEGG; bms:BRA1048; -.
DR KEGG; bsi:BS1330_II1040; -.
DR PATRIC; 17794931; VBIBruSui107850_3273.
DR eggNOG; COG1803; -.
DR HOGENOM; HOG000283729; -.
DR KO; K01734; -.
DR OMA; EPQPHDP; -.
DR ProtClustDB; PRK05234; -.
DR GO; GO:0008929; F:methylglyoxal synthase activity; IEA:HAMAP.
DR GO; GO:0019242; P:methylglyoxal biosynthetic process; IEA: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; MGS-like_dom; 1.
DR TIGRFAMs; TIGR00160; MGSA; 1.
DR PROSITE; PS01335; METHYLGLYOXAL_SYNTH; 1.
PE 3: Inferred from homology;
KW Complete proteome; Lyase.
FT CHAIN 1 125 Methylglyoxal synthase.
FT /FTId=PRO_0000178618.
FT ACT_SITE 65 65 By similarity.
SQ SEQUENCE 125 AA; 13546 MW; C8C2734C455C9060 CRC64;
MTQRLRIALI AHDQKKDDMV AFARAHEQAL SRYDIVATGT TGGLIQDACP SLNIHRVKSG
PLGGDQQIGA MIAEGTVEVL IFFIDPLSPL PHDVDVKALT RLGSVYDIPM ALNRATAEKL
VRALD
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