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 27-MAR-2024, entry version 103.
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; Bacillota; 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};
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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 KEGG; cac:CA_C1604; -.
DR PATRIC; fig|272562.8.peg.1803; -.
DR eggNOG; COG1803; Bacteria.
DR HOGENOM; CLU_120420_0_1_9; -.
DR OrthoDB; 9787147at2; -.
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; Methylglyoxal synthase-like domain; 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 NCBIfam; TIGR00160; MGSA; 1.
DR PANTHER; PTHR30492; METHYLGLYOXAL SYNTHASE; 1.
DR PANTHER; PTHR30492:SF0; METHYLGLYOXAL SYNTHASE; 1.
DR Pfam; PF02142; MGS; 1.
DR PIRSF; PIRSF006614; Methylglyox_syn; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 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
//
