MGSA_BURMS
ID MGSA_BURMS Reviewed; 130 AA.
AC A1V2G6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=BMASAVP1_A1079;
OS Burkholderia mallei (strain SAVP1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320388;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAVP1;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000526; ABM51200.1; -; Genomic_DNA.
DR RefSeq; WP_004186317.1; NC_008785.1.
DR AlphaFoldDB; A1V2G6; -.
DR SMR; A1V2G6; -.
DR GeneID; 56595098; -.
DR KEGG; bmv:BMASAVP1_A1079; -.
DR HOGENOM; CLU_120420_1_0_4; -.
DR OMA; RACDVHN; -.
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..130
FT /note="Methylglyoxal synthase"
FT /id="PRO_1000017794"
FT DOMAIN 1..130
FT /note="MGS-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT ACT_SITE 63
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 37..40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 57..58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
SQ SEQUENCE 130 AA; 13654 MW; 494D74B03DDE854E CRC64;
MSTPRIALIA HDAKKDDIVA LAGAYRATLA QCRLVATGTT GGRIAQAHGL DVERKLSGPL
GGDLQIGAEL ADGRVDIVIF LRDPMTAQPH DPDITALVRA CDVHDVPVAT NVATARVLLD
DLARRLTANA
