UniProt functional annotation for P0AC81

UniProt code: P0AC81.

Organism: Escherichia coli (strain K12).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
 
Function: Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (PubMed:10913283) (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response (PubMed:23536188). {ECO:0000269|PubMed:10913283, ECO:0000269|PubMed:23536188, ECO:0000305|PubMed:25670698}.
 
Catalytic activity: Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal; Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=4.4.1.5; Evidence={ECO:0000269|PubMed:10913283};
Cofactor: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:10913283}; Note=Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits. Is not active with zinc ions. {ECO:0000269|PubMed:10913283};
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2. {ECO:0000269|PubMed:25670698}.
Subunit: Homodimer. {ECO:0000269|PubMed:10913283}.
Induction: Repressed by NemR. Induced by reactive electrophilic species (RES) such as quinones, glyoxals and methylglyoxal (PubMed:23506073, PubMed:23646895). Up-regulated by HOCl (PubMed:23536188). {ECO:0000269|PubMed:23506073, ECO:0000269|PubMed:23536188, ECO:0000269|PubMed:23646895}.
Mass spectrometry: Mass=14919; Method=Electrospray; Evidence={ECO:0000269|PubMed:9628737};
Disruption phenotype: Deletion of the gene increases the HOCl sensitivity. Mutant is more sensitive to methylglyoxal treatment. {ECO:0000269|PubMed:23536188}.
Similarity: Belongs to the glyoxalase I family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.