ID MGSA_LATSS Reviewed; 140 AA. AC Q38WH3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 22-FEB-2023, entry version 86. 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=LCA_1157; OS Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei OS subsp. sakei). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Latilactobacillus. 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., Loux V., RA 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}. 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; CR936503; CAI55459.1; -; Genomic_DNA. DR RefSeq; WP_011374855.1; NC_007576.1. DR AlphaFoldDB; Q38WH3; -. DR SMR; Q38WH3; -. DR STRING; 314315.LCA_1157; -. DR EnsemblBacteria; CAI55459; CAI55459; LCA_1157. DR GeneID; 57132079; -. DR KEGG; lsa:LCA_1157; -. DR eggNOG; COG1803; Bacteria. DR HOGENOM; CLU_120420_1_0_9; -. DR OMA; RACDVHN; -. DR OrthoDB; 9787147at2; -. 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; 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 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 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..140 FT /note="Methylglyoxal synthase" FT /id="PRO_1000017815" FT DOMAIN 1..140 FT /note="MGS-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549" FT ACT_SITE 60 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549" FT BINDING 8 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549" FT BINDING 12 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549" FT BINDING 34..37 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549" FT BINDING 54..55 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549" FT BINDING 87 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-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 //