ID   MGSA_COXBR              Reviewed;         143 AA.
AC   A9ND61;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=COXBURSA331_A1097;
OS   Coxiella burnetii (strain RSA 331 / Henzerling II).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=360115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 331 / Henzerling II;
RA   Seshadri R., Samuel J.E.;
RT   "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT   burnetii isolates.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000890; ABX78112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9ND61; -.
DR   SMR; A9ND61; -.
DR   KEGG; cbs:COXBURSA331_A1097; -.
DR   HOGENOM; CLU_120420_0_1_6; -.
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..143
FT                   /note="Methylglyoxal synthase"
FT                   /id="PRO_1000081954"
FT   DOMAIN          1..143
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   143 AA;  16261 MW;  E7A7FCC79CA00254 CRC64;
     MTVKKIALVA HDRMKKELIE WIKKHQNLLK HHELYATGST GQAIEKTLNV TVTKMESGPL
     GGDLQLGVKI VNKEIDILIF FWDPLEAQPH DPDVRALLRI AVVWNLPVAC NASTADYLLT
     SPLFDSDYHP ETPDYEAYRN RII