ID A0A090IW25_9BACI Unreviewed; 135 AA.
AC A0A090IW25;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ECO:0000313|EMBL:CEE01857.1};
GN ORFNames=B4064_0576 {ECO:0000313|EMBL:KIO63101.1}, B4065_0539
GN {ECO:0000313|EMBL:KIO65614.1}, BT1A1_2035
GN {ECO:0000313|EMBL:CEE01857.1}, CQJ30_11270
GN {ECO:0000313|EMBL:AWI12681.1};
OS Caldibacillus thermoamylovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE01857.1, ECO:0000313|Proteomes:UP000040576};
RN [1] {ECO:0000313|EMBL:CEE01857.1, ECO:0000313|Proteomes:UP000040576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg Daniel;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000032071, ECO:0000313|Proteomes:UP000032078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4064 {ECO:0000313|EMBL:KIO63101.1,
RC ECO:0000313|Proteomes:UP000032078}, and B4065
RC {ECO:0000313|EMBL:KIO65614.1, ECO:0000313|Proteomes:UP000032071};
RA Krawcyk A.O., Berendsen E.M., Eijlander R.T., de Jong A., Wells-Bennik M.,
RA Kuipers O.P.;
RT "Draft Genome Sequences of Four Bacillus thermoamylovorans Strains,
RT Isolated From Food Products.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AWI12681.1, ECO:0000313|Proteomes:UP000244914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSBM {ECO:0000313|EMBL:AWI12681.1,
RC ECO:0000313|Proteomes:UP000244914};
RX PubMed=29625286; DOI=10.1016/j.biortech.2018.03.121;
RA Cai L., Zheng S.W., Shen Y.J., Zheng G.D., Liu H.T., Wu Z.Y.;
RT "Complete genome sequence provides insights into the biodrying-related
RT microbial function of Bacillus thermoamylovorans isolated from sewage
RT sludge biodrying material.";
RL Bioresour. Technol. 260:141-149(2018).
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}.
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DR EMBL; CP023704; AWI12681.1; -; Genomic_DNA.
DR EMBL; CCRF01000061; CEE01857.1; -; Genomic_DNA.
DR EMBL; JXLR01000097; KIO63101.1; -; Genomic_DNA.
DR EMBL; JXLS01000052; KIO65614.1; -; Genomic_DNA.
DR RefSeq; WP_034770616.1; NZ_JXLS01000052.1.
DR AlphaFoldDB; A0A090IW25; -.
DR STRING; 35841.B4167_0593; -.
DR KEGG; bthv:CQJ30_11270; -.
DR PATRIC; fig|35841.6.peg.3492; -.
DR eggNOG; COG1803; Bacteria.
DR Proteomes; UP000032071; Unassembled WGS sequence.
DR Proteomes; UP000032078; Unassembled WGS sequence.
DR Proteomes; UP000040576; Unassembled WGS sequence.
DR Proteomes; UP000244914; 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; 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:CEE01857.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000040576}.
FT DOMAIN 1..135
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 60
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549,
FT ECO:0000256|PIRSR:PIRSR006614-1"
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 54..55
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 135 AA; 15290 MW; 4AC6E34ECD5D19AB CRC64;
MNIALIAHDR KKDDLVQFVT AYRYIFEKHS LFATGTTGQR IIEATGLQVH RFQSGPLGGD
QEIGARIAKN EMDIVIFFRD PLTAQPHEPD VSALIRLADV YRVPIATNMG TAEVLIRGLE
RGDIDWREVI KNMRQ
//
