ID A0A1B6BBG8_9FIRM Unreviewed; 168 AA.
AC A0A1B6BBG8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=F3D3_1556 {ECO:0000313|EMBL:GAU76957.1};
OS Fusibacter sp. 3D3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU76957.1, ECO:0000313|Proteomes:UP000095197};
RN [1] {ECO:0000313|EMBL:GAU76957.1, ECO:0000313|Proteomes:UP000095197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D3 {ECO:0000313|EMBL:GAU76957.1,
RC ECO:0000313|Proteomes:UP000095197};
RA Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA Demergasso C.S.;
RT "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT arsenic level Ascotan salt flat in northern Chile.";
RL Submitted (SEP-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: 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:GAU76957.1}.
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DR EMBL; BDHH01000005; GAU76957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6BBG8; -.
DR STRING; 1048380.F3D3_1556; -.
DR OrthoDB; 9787147at2; -.
DR Proteomes; UP000095197; 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; IPR018148; Methylglyoxal_synth_AS.
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; PS01335; METHYLGLYOXAL_SYNTH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00549, ECO:0000313|EMBL:GAU76957.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095197}.
FT DOMAIN 8..168
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 73
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549,
FT ECO:0000256|PIRSR:PIRSR006614-1"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 47..50
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 67..68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
SQ SEQUENCE 168 AA; 18935 MW; 90BA7F89EAFC9D09 CRC64;
MSEKKMSHLI PAVKHIALIA HDSRKKDMIN WCDENKDSLS KHFLYGTGTT AKMISEATEL
PVRGVKSGPL GGDQQIGSKI VEGEINFMIF FWDPLSMHPH DPDVKALLRI ATLYNIPIAT
NIATADYLLT SIHMNQPYEG KLINFDQYLN RKIELECQKS KAEQPSPL
//
