ID B8E059_DICTD Unreviewed; 153 AA.
AC B8E059;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Methylglyoxal synthase {ECO:0000256|HAMAP-Rule:MF_00549};
DE Short=MGS {ECO:0000256|HAMAP-Rule:MF_00549};
DE EC=4.2.3.3 {ECO:0000256|HAMAP-Rule:MF_00549};
GN Name=mgsA {ECO:0000256|HAMAP-Rule:MF_00549};
GN OrderedLocusNames=Dtur_0861 {ECO:0000313|EMBL:ACK42142.1};
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC Dictyoglomus.
OX NCBI_TaxID=515635 {ECO:0000313|EMBL:ACK42142.1, ECO:0000313|Proteomes:UP000007719};
RN [1] {ECO:0000313|Proteomes:UP000007719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310 {ECO:0000313|Proteomes:UP000007719};
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
CC -!- FUNCTION: Catalyzes the formation of methylglyoxal from
CC dihydroxyacetone phosphate. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00549};
CC -!- SIMILARITY: Belongs to the methylglyoxal synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_00549}.
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DR EMBL; CP001251; ACK42142.1; -; Genomic_DNA.
DR RefSeq; WP_012583226.1; NC_011661.1.
DR RefSeq; YP_002352756.1; NC_011661.1.
DR AlphaFoldDB; B8E059; -.
DR STRING; 515635.Dtur_0861; -.
DR EnsemblBacteria; ACK42142; ACK42142; Dtur_0861.
DR KEGG; dtu:Dtur_0861; -.
DR PATRIC; fig|515635.4.peg.900; -.
DR eggNOG; COG1803; Bacteria.
DR HOGENOM; CLU_120420_0_1_0; -.
DR InParanoid; B8E059; -.
DR OrthoDB; 9787147at2; -.
DR Proteomes; UP000007719; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008929; F:methylglyoxal synthase activity; IBA:GO_Central.
DR GO; GO:0019242; P:methylglyoxal biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00549, ECO:0000313|EMBL:ACK42142.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007719}.
FT DOMAIN 6..153
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 71
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549,
FT ECO:0000256|PIRSR:PIRSR006614-1"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 45..48
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 65..66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
SQ SEQUENCE 153 AA; 17332 MW; E9F9E0C618F754B8 CRC64;
MGYREIIMGK QKRIALVAHD NKKQELLEWA KFNKGTLANH ILYATGTTGD IIERELGLKV
IKFYSGPLGG DQQIGAKIAE GEIDFLIFFW DPLEPLPHDP DVKALLRIAV VWNIPIASNR
ATADFIISSP LMNTEYVRLV PDYQGYIHRK INL
//
