ID MGSA_ECOLI Reviewed; 152 AA. AC P0A731; P37066; P75872; Q8XD91; Q9R7Q3; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 1. DT 27-MAR-2024, entry version 129. 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, ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, ECO:0000269|PubMed:9665712}; GN Name=mgsA {ECO:0000255|HAMAP-Rule:MF_00549}; Synonyms=yccG; GN OrderedLocusNames=b0963, JW5129; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2542273; DOI=10.1016/s0021-9258(18)83182-9; RA Wood E.R., Matson S.W.; RT "The molecular cloning of the gene encoding the Escherichia coli 75-kDa RT helicase and the determination of its nucleotide sequence and gentic map RT position."; RL J. Biol. Chem. 264:8297-8303(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION. RX PubMed=9489667; DOI=10.1046/j.1365-2958.1998.00700.x; RA Totemeyer S., Booth N.A., Nichols W.W., Dunbar B., Booth I.R.; RT "From famine to feast: the role of methylglyoxal production in Escherichia RT coli."; RL Mol. Microbiol. 27:553-562(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP IDENTIFICATION. RX PubMed=7984428; DOI=10.1093/nar/22.22.4756; RA Borodovsky M., Rudd K.E., Koonin E.V.; RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial RT genome."; RL Nucleic Acids Res. 22:4756-4767(1994). RN [7] RP FUNCTION, ACTIVITY REGULATION, PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF RP ASP-20; ASP-71; ASP-91 AND ASP-101, BIOPHYSICOCHEMICAL PROPERTIES, AND RP ACTIVE SITE. RX PubMed=9665712; DOI=10.1021/bi980409p; RA Saadat D., Harrison D.H.T.; RT "Identification of catalytic bases in the active site of Escherichia coli RT methylglyoxal synthase: cloning, expression, and functional RT characterization of conserved aspartic acid residues."; RL Biochemistry 37:10074-10086(1998). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT. RX PubMed=10368300; DOI=10.1016/s0969-2126(99)80041-0; RA Saadat D., Harrison D.H.T.; RT "The crystal structure of methylglyoxal synthase from Escherichia coli."; RL Structure 7:309-317(1999). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG RP 2-PHOSPHOGLYCOLATE, ACTIVE SITE, AND SUBUNIT. RX PubMed=10715115; DOI=10.1021/bi992666f; RA Saadat D., Harrison D.H.T.; RT "Mirroring perfection: the structure of methylglyoxal synthase complexed RT with the competitive inhibitor 2-phosphoglycolate."; RL Biochemistry 39:2950-2960(2000). RN [10] {ECO:0007744|PDB:1IK4} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG RP PHOSPHOGLYCOLOHYDROXAMATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, ACTIVE SITE, AND SUBUNIT. RX PubMed=11389594; DOI=10.1021/bi0028237; RA Marks G.T., Harris T.K., Massiah M.A., Mildvan A.S., Harrison D.H.; RT "Mechanistic implications of methylglyoxal synthase complexed with RT phosphoglycolohydroxamic acid as observed by X-ray crystallography and NMR RT spectroscopy."; RL Biochemistry 40:6805-6818(2001). RN [11] {ECO:0007744|PDB:1S89, ECO:0007744|PDB:1S8A} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANTS ASN/GLN-98 IN COMPLEX RP WITH SUBSTRATE ANALOG 2-PHOSPHOGLYCOLATE, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACTIVE SITE, SUBUNIT, RP AND MUTAGENESIS OF HIS-98. RX PubMed=15049687; DOI=10.1021/bi035838o; RA Marks G.T., Susler M., Harrison D.H.; RT "Mutagenic studies on histidine 98 of methylglyoxal synthase: effects on RT mechanism and conformational change."; RL Biochemistry 43:3802-3813(2004). CC -!- FUNCTION: Catalyzes the formation of methylglyoxal from CC dihydroxyacetone phosphate. {ECO:0000255|HAMAP-Rule:MF_00549, CC ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, CC ECO:0000269|PubMed:9665712}. 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, ECO:0000269|PubMed:11389594, CC ECO:0000269|PubMed:15049687, ECO:0000269|PubMed:9665712}; CC -!- ACTIVITY REGULATION: Inhibited by inorganic phosphate ions CC (PubMed:9665712, PubMed:15049687). Competitively inhibited by CC phosphoglycolate (PubMed:15049687). Competitively inhibited by CC phosphoglycolohydroxamate (PubMed:11389594). CC {ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, CC ECO:0000269|PubMed:9665712}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.2 mM for dihydroxyacetone phosphate CC {ECO:0000269|PubMed:9665712}; CC Note=kcat is 220 sec(-1) with dihydroxyacetone phosphate as CC substrate. {ECO:0000269|PubMed:9665712}; CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:15049687}; CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:10368300, CC ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, CC ECO:0000269|PubMed:15049687}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the methylglyoxal synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000305}. 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; J04726; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Y11249; CAA72119.1; -; Genomic_DNA. DR EMBL; U00096; AAC74049.2; -; Genomic_DNA. DR EMBL; AP009048; BAA35728.2; -; Genomic_DNA. DR PIR; B64837; B64837. DR RefSeq; NP_415483.2; NC_000913.3. DR RefSeq; WP_000424181.1; NZ_STEB01000006.1. DR PDB; 1B93; X-ray; 1.90 A; A/B/C=1-152. DR PDB; 1EGH; X-ray; 2.00 A; A/B/C/D/E/F=1-152. DR PDB; 1IK4; X-ray; 2.00 A; A/B/C/D/E/F=1-152. DR PDB; 1S89; X-ray; 2.22 A; A/B/C/D/E/F=1-152. DR PDB; 1S8A; X-ray; 2.20 A; A/B/C/D/E/F=1-152. DR PDBsum; 1B93; -. DR PDBsum; 1EGH; -. DR PDBsum; 1IK4; -. DR PDBsum; 1S89; -. DR PDBsum; 1S8A; -. DR AlphaFoldDB; P0A731; -. DR SMR; P0A731; -. DR BioGRID; 4260938; 11. DR BioGRID; 849948; 1. DR DIP; DIP-48252N; -. DR STRING; 511145.b0963; -. DR jPOST; P0A731; -. DR PaxDb; 511145-b0963; -. DR EnsemblBacteria; AAC74049; AAC74049; b0963. DR GeneID; 75204054; -. DR GeneID; 945574; -. DR KEGG; ecj:JW5129; -. DR KEGG; eco:b0963; -. DR PATRIC; fig|1411691.4.peg.1311; -. DR EchoBASE; EB2213; -. DR eggNOG; COG1803; Bacteria. DR HOGENOM; CLU_120420_0_1_6; -. DR InParanoid; P0A731; -. DR OMA; RICDVHN; -. DR OrthoDB; 9787147at2; -. DR PhylomeDB; P0A731; -. DR BioCyc; EcoCyc:METHGLYSYN-MONOMER; -. DR BioCyc; MetaCyc:METHGLYSYN-MONOMER; -. DR BRENDA; 4.2.3.3; 2026. DR SABIO-RK; P0A731; -. DR EvolutionaryTrace; P0A731; -. DR PRO; PR:P0A731; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0008929; F:methylglyoxal synthase activity; IDA:EcoCyc. DR GO; GO:0019242; P:methylglyoxal biosynthetic process; IMP:EcoCyc. DR GO; GO:0034214; P:protein hexamerization; IDA:EcoCyc. 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Lyase; KW Reference proteome. FT CHAIN 1..152 FT /note="Methylglyoxal synthase" FT /id="PRO_0000178625" FT DOMAIN 6..152 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 ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, FT ECO:0000269|PubMed:15049687, ECO:0000269|PubMed:9665712" FT BINDING 19 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549, FT ECO:0000269|PubMed:11389594, ECO:0007744|PDB:1IK4" FT BINDING 23 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549, FT ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, FT ECO:0000269|PubMed:15049687, ECO:0007744|PDB:1EGH, FT ECO:0007744|PDB:1IK4, ECO:0007744|PDB:1S89, FT ECO:0007744|PDB:1S8A" FT BINDING 45..48 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549, FT ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, FT ECO:0000269|PubMed:15049687, ECO:0007744|PDB:1EGH, FT ECO:0007744|PDB:1IK4, ECO:0007744|PDB:1S89, FT ECO:0007744|PDB:1S8A" FT BINDING 65..66 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549, FT ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, FT ECO:0000269|PubMed:15049687, ECO:0007744|PDB:1EGH, FT ECO:0007744|PDB:1IK4, ECO:0007744|PDB:1S89, FT ECO:0007744|PDB:1S8A" FT BINDING 98 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549, FT ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, FT ECO:0007744|PDB:1EGH, ECO:0007744|PDB:1IK4" FT MUTAGEN 20 FT /note="D->E: Strongly decreased catalytic efficiency." FT /evidence="ECO:0000269|PubMed:9665712" FT MUTAGEN 20 FT /note="D->N: Causes inhibition by substrate leading to loss FT of enzyme activity." FT /evidence="ECO:0000269|PubMed:9665712" FT MUTAGEN 71 FT /note="D->E,N: Strongly decreased catalytic efficiency." FT /evidence="ECO:0000269|PubMed:9665712" FT MUTAGEN 91 FT /note="D->E: Strongly decreased catalytic efficiency." FT /evidence="ECO:0000269|PubMed:9665712" FT MUTAGEN 91 FT /note="D->N: Causes inhibition by substrate leading to loss FT of enzyme activity." FT /evidence="ECO:0000269|PubMed:9665712" FT MUTAGEN 98 FT /note="H->N,Q: Strongly decreased catalytic efficiency." FT /evidence="ECO:0000269|PubMed:15049687" FT MUTAGEN 101 FT /note="D->E,N: Strongly decreased catalytic efficiency." FT /evidence="ECO:0000269|PubMed:9665712" FT CONFLICT 1..2 FT /note="ME -> WK (in Ref. 1; J04726)" FT /evidence="ECO:0000305" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:1B93" FT STRAND 13..18 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 23..32 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 34..37 FT /evidence="ECO:0007829|PDB:1B93" FT STRAND 40..45 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 48..56 FT /evidence="ECO:0007829|PDB:1B93" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 70..79 FT /evidence="ECO:0007829|PDB:1B93" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 99..111 FT /evidence="ECO:0007829|PDB:1B93" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 120..127 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 130..133 FT /evidence="ECO:0007829|PDB:1B93" FT STRAND 136..141 FT /evidence="ECO:0007829|PDB:1B93" FT HELIX 143..147 FT /evidence="ECO:0007829|PDB:1B93" SQ SEQUENCE 152 AA; 16919 MW; 85157193BD4CE72D CRC64; MELTTRTLPA RKHIALVAHD HCKQMLMSWV ERHQPLLEQH VLYATGTTGN LISRATGMNV NAMLSGPMGG DQQVGALISE GKIDVLIFFW DPLNAVPHDP DVKALLRLAT VWNIPVATNV ATADFIIQSP HFNDAVDILI PDYQRYLADR LK //