MGSA_ECOLI
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 03-AUG-2022, entry version 121.
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; Proteobacteria; 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}.
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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; P0A731; -.
DR PRIDE; P0A731; -.
DR EnsemblBacteria; AAC74049; AAC74049; b0963.
DR EnsemblBacteria; BAA35728; BAA35728; BAA35728.
DR GeneID; 66670761; -.
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; RACDVHN; -.
DR PhylomeDB; P0A731; -.
DR BioCyc; EcoCyc:METHGLYSYN-MON; -.
DR BioCyc; MetaCyc:METHGLYSYN-MON; -.
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; -; 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 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
