ID   MGSA_CLOAB              Reviewed;         145 AA.
AC   Q97IN6;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 97.
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}; OrderedLocusNames=CA_C1604;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK79571.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE001437; AAK79571.1; ALT_INIT; Genomic_DNA.
DR   PIR; H97097; H97097.
DR   RefSeq; NP_348231.1; NC_003030.1.
DR   AlphaFoldDB; Q97IN6; -.
DR   SMR; Q97IN6; -.
DR   STRING; 272562.CA_C1604; -.
DR   EnsemblBacteria; AAK79571; AAK79571; CA_C1604.
DR   KEGG; cac:CA_C1604; -.
DR   PATRIC; fig|272562.8.peg.1803; -.
DR   eggNOG; COG1803; Bacteria.
DR   HOGENOM; CLU_120420_0_1_9; -.
DR   OMA; RACDVHN; -.
DR   OrthoDB; 1726279at2; -.
DR   Proteomes; UP000000814; Chromosome.
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; Reference proteome.
FT   CHAIN           1..145
FT                   /note="Methylglyoxal synthase"
FT                   /id="PRO_0000178621"
FT   DOMAIN          1..145
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   ACT_SITE        64
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         58..59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
SQ   SEQUENCE   145 AA;  16377 MW;  C008B3319119E058 CRC64;
     MNSKKKIALV AHDNRKKALI SWCEANSEVL SNHSLCGTGT TAKLIKEATG LEVFPYKSGP
     MGGDQQIGAA IVNEDIDFMI FFWDPLTAQP HDPDVKALLR ISVLYDIPIA MNESTAEFLI
     KSPIMKEQHE RHIIDYYQKI RKDNF