ID A0A1M7GRB6_9FIRM Unreviewed; 131 AA.
AC A0A1M7GRB6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN02746066_01076 {ECO:0000313|EMBL:SHM18924.1};
OS Anaerosporobacter mobilis DSM 15930.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerosporobacter.
OX NCBI_TaxID=1120996 {ECO:0000313|EMBL:SHM18924.1, ECO:0000313|Proteomes:UP000184038};
RN [1] {ECO:0000313|EMBL:SHM18924.1, ECO:0000313|Proteomes:UP000184038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15930 {ECO:0000313|EMBL:SHM18924.1,
RC ECO:0000313|Proteomes:UP000184038};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRCP01000007; SHM18924.1; -; Genomic_DNA.
DR RefSeq; WP_073284173.1; NZ_FRCP01000007.1.
DR AlphaFoldDB; A0A1M7GRB6; -.
DR STRING; 1120996.SAMN02746066_01076; -.
DR OrthoDB; 9787147at2; -.
DR Proteomes; UP000184038; 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:UP000184038}.
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; 14622 MW; FA64C66B3B8A0C8F CRC64;
MNIGMIAHDA KKKLMQNFCI AYRGILSKNE LFATGTTGRL IEEVTNLNVH KYLAGHLGGE
QQLGAQIEHN QIDIVIFLRD PLTPKSHEPD VNNVVQLCDT HNIPLATNLA TAELLIKALD
RGDLEWREAL K
//
