ID   MGSA_TRESO              Reviewed;         158 AA.
AC   P58761;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 58.
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};
OS   Treponema socranskii.
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=53419;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35536 / JCM 8157 / VPI DR56BRIII6;
RX   PubMed=11470357; DOI=10.1111/j.1574-6968.2001.tb10752.x;
RA   Heuner K., Bergmann I., Heckenbach K., Goebel U.B.;
RT   "Proteolytic activity among various oral Treponema species and cloning of a
RT   prtP-like gene of Treponema socranskii subsp. socranskii.";
RL   FEMS Microbiol. Lett. 201:169-176(2001).
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}.
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DR   EMBL; AJ272337; CAC81260.1; -; Genomic_DNA.
DR   AlphaFoldDB; P58761; -.
DR   SMR; P58761; -.
DR   GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019242; P:methylglyoxal biosynthetic process; IEA:UniProtKB-UniRule.
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; 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   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..158
FT                   /note="Methylglyoxal synthase"
FT                   /id="PRO_0000178651"
FT   DOMAIN          1..158
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   ACT_SITE        69
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         63..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
SQ   SEQUENCE   158 AA;  17877 MW;  666D521E567AC2BD CRC64;
     MRRKLRIALV AHDNRKADIV DWALNNAEML SQHRLFGTGT TGTLVRESFM KRGIASDITC
     MHSGPMGGDA EIAALVVRKE IDFAVFFIDD LNPQPHEADI QMLLRQCRIH NIPIACNRYS
     ADLMITSSLW DDAGYVPKDP IYAPFDRKAF EESLKVKE