MGSA_THEMA
ID MGSA_THEMA Reviewed; 155 AA.
AC Q9X0R7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=TM_1185;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAD36260.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000512; AAD36260.1; ALT_INIT; Genomic_DNA.
DR PIR; G72284; G72284.
DR RefSeq; NP_228990.1; NC_000853.1.
DR PDB; 1VMD; X-ray; 2.06 A; A/B=1-155.
DR PDBsum; 1VMD; -.
DR AlphaFoldDB; Q9X0R7; -.
DR SMR; Q9X0R7; -.
DR STRING; 243274.THEMA_08410; -.
DR PRIDE; Q9X0R7; -.
DR EnsemblBacteria; AAD36260; AAD36260; TM_1185.
DR KEGG; tma:TM1185; -.
DR eggNOG; COG1803; Bacteria.
DR InParanoid; Q9X0R7; -.
DR OMA; RACDVHN; -.
DR EvolutionaryTrace; Q9X0R7; -.
DR Proteomes; UP000008183; 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; -; 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; Lyase; Reference proteome.
FT CHAIN 1..155
FT /note="Methylglyoxal synthase"
FT /id="PRO_0000178648"
FT DOMAIN 1..155
FT /note="MGS-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT ACT_SITE 64
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 38..41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 58..59
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1VMD"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:1VMD"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1VMD"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:1VMD"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1VMD"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1VMD"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:1VMD"
SQ SEQUENCE 155 AA; 17641 MW; A60A600F5D144205 CRC64;
MDKKKRIALI AHDRRKRDLL EWVSFNLGTL SKHELYATGT TGALLQEKLG LKVHRLKSGP
LGGDQQIGAM IAEGKIDVLI FFWDPLEPQA HDVDVKALIR IATVYNIPVA ITRSTADFLI
SSPLMNDVYE KIQIDYEEEL ERRIRKVVEG EEEET
