ID   MGSA_LACSS              Reviewed;         140 AA.
AC   Q38WH3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   10-APR-2019, 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=LCA_1157;
OS   Lactobacillus sakei subsp. sakei (strain 23K).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=314315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23K;
RX   PubMed=16273110; DOI=10.1038/nbt1160;
RA   Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA   Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R.,
RA   Loux V., Zagorec M.;
RT   "The complete genome sequence of the meat-borne lactic acid bacterium
RT   Lactobacillus sakei 23K.";
RL   Nat. Biotechnol. 23:1527-1533(2005).
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; CR936503; CAI55459.1; -; Genomic_DNA.
DR   RefSeq; WP_011374855.1; NC_007576.1.
DR   ProteinModelPortal; Q38WH3; -.
DR   SMR; Q38WH3; -.
DR   STRING; 314315.LCA_1157; -.
DR   EnsemblBacteria; CAI55459; CAI55459; LCA_1157.
DR   GeneID; 29637137; -.
DR   KEGG; lsa:LCA_1157; -.
DR   eggNOG; ENOG4108Z5K; Bacteria.
DR   eggNOG; COG1803; LUCA.
DR   KO; K01734; -.
DR   OMA; RACDVHN; -.
DR   OrthoDB; 1726279at2; -.
DR   Proteomes; UP000002707; 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   Complete proteome; Lyase; Reference proteome.
FT   CHAIN         1    140       Methylglyoxal synthase.
FT                                /FTId=PRO_1000017815.
FT   DOMAIN        1    140       MGS-like. {ECO:0000255|HAMAP-
FT                                Rule:MF_00549}.
FT   REGION       34     37       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00549}.
FT   REGION       54     55       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00549}.
FT   ACT_SITE     60     60       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00549}.
FT   BINDING       8      8       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00549}.
FT   BINDING      12     12       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00549}.
FT   BINDING      87     87       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00549}.
SQ   SEQUENCE   140 AA;  15275 MW;  B6C063ED6E2DECA3 CRC64;
     MKIALIAHDR QKPLIVKLAT AYQPILAQHE LFATGTTGQK IIDATGLSVK RFKSGPLGGD
     QQIGALISEN KMDLVIFLRD PLTAQPHEPD VNALIRLSDV YEVPLATNIG TAEVLLRGLD
     QGLMAFREVV HDQDSNPINL
//