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 28-MAR-2018, entry version 67. 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: Glycerone phosphate = methylglyoxal + CC phosphate. {ECO:0000255|HAMAP-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 ProteinModelPortal; Q38WH3; -. DR SMR; Q38WH3; -. DR STRING; 314315.LSA1157; -. 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; POG091H04UH; -. DR Proteomes; UP000002707; Chromosome. DR GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-EC. DR GO; GO:0019242; P:methylglyoxal biosynthetic process; IEA:InterPro. 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 //