ID E9CPY2_9GAMM Unreviewed; 152 AA.
AC E9CPY2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
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:EFW11538.1};
GN ORFNames=SSYM_2635 {ECO:0000313|EMBL:EFW11538.1};
OS Serratia symbiotica str. Tucson.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia; Serratia symbiotica.
OX NCBI_TaxID=914128 {ECO:0000313|EMBL:EFW11538.1, ECO:0000313|Proteomes:UP000013568};
RN [1] {ECO:0000313|Proteomes:UP000013568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson {ECO:0000313|Proteomes:UP000013568};
RX PubMed=21266540;
RA Burke G.R., Moran N.A.;
RT "Massive genomic decay in Serratia symbiotica, a recently evolved symbiont
RT of aphids.";
RL Genome Biol. Evol. 3:195-208(2011).
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|ARBA:ARBA00006287, ECO:0000256|HAMAP-Rule:MF_00549}.
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DR EMBL; GL636126; EFW11538.1; -; Genomic_DNA.
DR RefSeq; WP_006709749.1; NZ_GL636126.1.
DR AlphaFoldDB; E9CPY2; -.
DR HOGENOM; CLU_120420_0_1_6; -.
DR Proteomes; UP000013568; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000013568}.
FT DOMAIN 1..152
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 71
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549,
FT ECO:0000256|PIRSR:PIRSR006614-1"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 45..48
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 65..66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
SQ SEQUENCE 152 AA; 16895 MW; 0E25380326D3052F CRC64;
MELTTRTIAA CKHIALVAHD HRKQELLKWV ESHKAILVKH LLYATGTTGN LIHQASGISV
QSMLSGPMGG DQQIGALIAE GKIDMLIFFW DPLNAVPHDP DVKALLRLAT VWNIPVATNR
STADFLIDSS LFNGTVEIAI PDYRRYLQER LK
//
