MGSA_BRUA1
ID MGSA_BRUA1 Reviewed; 125 AA.
AC B2SC33; P0A3Q4; Q44615; Q576R7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Methylglyoxal synthase {ECO:0000255|HAMAP-Rule:MF_00549};
DE Short=MGS {ECO:0000255|HAMAP-Rule:MF_00549};
DE EC=4.2.3.3 {ECO:0000255|HAMAP-Rule:MF_00549};
GN Name=mgsA {ECO:0000255|HAMAP-Rule:MF_00549};
GN OrderedLocusNames=BAbS19_II09350;
OS Brucella abortus (strain S19).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=430066;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7592399; DOI=10.1128/jb.177.21.6297-6300.1995;
RA Essenberg R.C.;
RT "Cloning and characterization of the glucokinase gene of Brucella abortus
RT 19 and identification of three other genes.";
RL J. Bacteriol. 177:6297-6300(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S19;
RX PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA Bricker B., Yu G., Du L., Sobral B.W.;
RT "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT virulent strains yields candidate virulence genes.";
RL PLoS ONE 3:E2193-E2193(2008).
CC -!- FUNCTION: Catalyzes the formation of methylglyoxal from
CC dihydroxyacetone phosphate. {ECO:0000255|HAMAP-Rule:MF_00549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate;
CC Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57642; EC=4.2.3.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00549};
CC -!- SIMILARITY: Belongs to the methylglyoxal synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00549}.
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DR EMBL; U21919; AAC43671.1; -; Genomic_DNA.
DR EMBL; CP000888; ACD74420.1; -; Genomic_DNA.
DR RefSeq; WP_002965604.1; NC_010740.1.
DR AlphaFoldDB; B2SC33; -.
DR SMR; B2SC33; -.
DR EnsemblBacteria; ACD74420; ACD74420; BAbS19_II09350.
DR GeneID; 45126347; -.
DR GeneID; 55592669; -.
DR KEGG; bmc:BAbS19_II09350; -.
DR HOGENOM; CLU_120420_1_0_5; -.
DR OMA; RACDVHN; -.
DR Proteomes; UP000002565; Chromosome 2.
DR GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019242; P:methylglyoxal biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01422; MGS; 1.
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 InterPro; IPR036914; MGS-like_dom_sf.
DR PANTHER; PTHR30492; PTHR30492; 1.
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.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Lyase.
FT CHAIN 1..125
FT /note="Methylglyoxal synthase"
FT /id="PRO_1000128979"
FT DOMAIN 1..125
FT /note="MGS-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT ACT_SITE 65
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 38..41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 59..60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
SQ SEQUENCE 125 AA; 13546 MW; C8C2734C455C9060 CRC64;
MTQRLRIALI AHDQKKDDMV AFARAHEQAL SRYDIVATGT TGGLIQDACP SLNIHRVKSG
PLGGDQQIGA MIAEGTVEVL IFFIDPLSPL PHDVDVKALT RLGSVYDIPM ALNRATAEKL
VRALD