ID   MGSA_ALISL              Reviewed;         151 AA.
AC   B6EI79;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=VSAL_I2133;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(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; FM178379; CAQ79818.1; -; Genomic_DNA.
DR   RefSeq; WP_012550659.1; NC_011312.1.
DR   AlphaFoldDB; B6EI79; -.
DR   SMR; B6EI79; -.
DR   STRING; 316275.VSAL_I2133; -.
DR   EnsemblBacteria; CAQ79818; CAQ79818; VSAL_I2133.
DR   KEGG; vsa:VSAL_I2133; -.
DR   eggNOG; COG1803; Bacteria.
DR   HOGENOM; CLU_120420_0_1_6; -.
DR   OMA; RACDVHN; -.
DR   OrthoDB; 1726279at2; -.
DR   Proteomes; UP000001730; Chromosome 1.
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..151
FT                   /note="Methylglyoxal synthase"
FT                   /id="PRO_1000128972"
FT   DOMAIN          6..151
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   ACT_SITE        71
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         45..48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         65..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
SQ   SEQUENCE   151 AA;  16878 MW;  08A7F1FCE6A277C2 CRC64;
     MKKTTRIVPA HKHIALVAHD NYKAELLRWV KENKEALQGH FLYATGTTGH LLSKETGLAI
     KSLLSGPMGG DQQLGALISE GKIDMMIFFW DPLNAVPHDP DVKALLRIAT VWNVPVAMNR
     SSAKFMISSP RMTQEIEIEI PDYPAYLAER I