ID   MGSA_THET8              Reviewed;         126 AA.
AC   Q5SHD6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=TTHA1794;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of methylglyoxal synthase from Thermus thermophilus
RT   HB8.";
RL   Submitted (AUG-2005) to the PDB data bank.
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; AP008226; BAD71617.1; -; Genomic_DNA.
DR   RefSeq; WP_011228922.1; NC_006461.1.
DR   RefSeq; YP_145060.1; NC_006461.1.
DR   PDB; 1WO8; X-ray; 1.70 A; A/B/C/D/E/F=1-126.
DR   PDBsum; 1WO8; -.
DR   AlphaFoldDB; Q5SHD6; -.
DR   SMR; Q5SHD6; -.
DR   STRING; 300852.55773176; -.
DR   EnsemblBacteria; BAD71617; BAD71617; BAD71617.
DR   GeneID; 3168681; -.
DR   KEGG; ttj:TTHA1794; -.
DR   PATRIC; fig|300852.9.peg.1765; -.
DR   eggNOG; COG1803; Bacteria.
DR   HOGENOM; CLU_120420_1_0_0; -.
DR   OMA; RACDVHN; -.
DR   PhylomeDB; Q5SHD6; -.
DR   EvolutionaryTrace; Q5SHD6; -.
DR   Proteomes; UP000000532; Chromosome.
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; 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..126
FT                   /note="Methylglyoxal synthase"
FT                   /id="PRO_1000017830"
FT   DOMAIN          1..126
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   ACT_SITE        61
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         35..38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         55..56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   HELIX           13..22
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   HELIX           24..27
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   HELIX           36..46
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   TURN            56..59
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   HELIX           60..69
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   HELIX           89..101
FT                   /evidence="ECO:0007829|PDB:1WO8"
FT   HELIX           110..122
FT                   /evidence="ECO:0007829|PDB:1WO8"
SQ   SEQUENCE   126 AA;  13380 MW;  C13C4F5DAD5F6156 CRC64;
     MKALALIAHD AKKDEMVAFC LRHKDVLARY PLLATGTTGA RIQEATGLAV ERVLSGPLGG
     DLQIGARVAE GKVLAVVFLQ DPLTAKPHEP DVQALMRVCN VHGVPLATNL VAAEALIAWI
     RKGTPQ