ID R9KG62_9FIRM Unreviewed; 131 AA.
AC R9KG62;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 ORFNames=C810_02714 {ECO:0000313|EMBL:EOS45440.1};
OS Lachnospiraceae bacterium A2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=397290 {ECO:0000313|EMBL:EOS45440.1, ECO:0000313|Proteomes:UP000014150};
RN [1] {ECO:0000313|EMBL:EOS45440.1, ECO:0000313|Proteomes:UP000014150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2 {ECO:0000313|EMBL:EOS45440.1,
RC ECO:0000313|Proteomes:UP000014150};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium A2.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00549}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS45440.1}.
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DR EMBL; ASSX01000013; EOS45440.1; -; Genomic_DNA.
DR AlphaFoldDB; R9KG62; -.
DR STRING; 397290.C810_02714; -.
DR PATRIC; fig|397290.3.peg.3005; -.
DR eggNOG; COG1803; Bacteria.
DR HOGENOM; CLU_120420_1_0_9; -.
DR OrthoDB; 9787147at2; -.
DR Proteomes; UP000014150; Unassembled WGS sequence.
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; Methylglyoxal synthase-like domain; 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 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; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00549};
KW Reference proteome {ECO:0000313|Proteomes:UP000014150}.
FT DOMAIN 1..131
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 34..37
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
SQ SEQUENCE 131 AA; 14686 MW; 9D5A9A155E2512B9 CRC64;
MNIGLIAHDS KKKLMQNFCI AYRGILCKND LFATGTTGRL IEEVTNLSIH KYLAGHLGGA
QQLGAQIEHN QIDLVIFLRD PLTPKSHEPD VNNVVHLCDT HNIPLATNLA TAELLIKSLD
RGDLEWREMY K
//
