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Database: UniProt
Entry: A0A061AJE5_9MOLU
LinkDB: A0A061AJE5_9MOLU
Original site: A0A061AJE5_9MOLU 
ID   A0A061AJE5_9MOLU        Unreviewed;       122 AA.
AC   A0A061AJE5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   13-SEP-2023, entry version 39.
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:CDR31112.1};
GN   ORFNames=Aocu_10390 {ECO:0000313|EMBL:CDR31112.1};
OS   Acholeplasma oculi.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=35623 {ECO:0000313|EMBL:CDR31112.1, ECO:0000313|Proteomes:UP000032434};
RN   [1] {ECO:0000313|Proteomes:UP000032434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kube M.;
RL   Submitted (MAY-2014) 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}.
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DR   EMBL; LK028559; CDR31112.1; -; Genomic_DNA.
DR   RefSeq; WP_045749563.1; NZ_UFRU01000001.1.
DR   AlphaFoldDB; A0A061AJE5; -.
DR   STRING; 35623.Aocu_10390; -.
DR   KEGG; aoc:Aocu_10390; -.
DR   PATRIC; fig|35623.3.peg.1039; -.
DR   HOGENOM; CLU_120420_1_0_14; -.
DR   InParanoid; A0A061AJE5; -.
DR   OrthoDB; 9787147at2; -.
DR   Proteomes; UP000032434; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032434}.
FT   DOMAIN          1..122
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   122 AA;  13500 MW;  E2191BEFA7896B86 CRC64;
     MKIALIAHDK KKDLIIEFSK LHEAYLKTHQ LYATGTTGKK IMEHTNLSVN LKKSGPLGGD
     QEIGSMIANG KIDMVIFFRD PLTAQPHEPD VSALLRLCDV YNIPLATNPK AAELFLGELK
     SK
//
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