MGSA_SALPK
ID MGSA_SALPK Reviewed; 152 AA.
AC B5BBK4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=SSPA1647;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(2009).
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; FM200053; CAR59839.1; -; Genomic_DNA.
DR RefSeq; WP_000424187.1; NC_011147.1.
DR AlphaFoldDB; B5BBK4; -.
DR SMR; B5BBK4; -.
DR KEGG; sek:SSPA1647; -.
DR HOGENOM; CLU_120420_0_1_6; -.
DR OMA; RACDVHN; -.
DR Proteomes; UP000001869; 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 3: Inferred from homology;
KW Lyase.
FT CHAIN 1..152
FT /note="Methylglyoxal synthase"
FT /id="PRO_1000129008"
FT DOMAIN 6..152
FT /note="MGS-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT ACT_SITE 71
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 45..48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 65..66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
SQ SEQUENCE 152 AA; 16991 MW; EE91B36C190FD0A6 CRC64;
MELTTRTLPT RKHIALVAHD HCKQMLMNWV ERHQPLLEKH VLYATGTTGN LIQRATGMDV
NAMLSGPMGG DQQVGALISE GKIDVLIFFW DPLNAVPHDP DVKALLRLAT VWNIPVATNV
STADFIIQSP HFNDAVDILI PDYARYLAER LK
