A0A2D2M7T4 · A0A2D2M7T4_9PSED
- ProteinLactoylglutathione lyase
- GenegloA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids173 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic activity
- (R)-S-lactoylglutathione = methylglyoxal + glutathione
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 nickel ion per subunit.
Note: Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.
Pathway
Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 93 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 120 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Active site | 166 | Proton donor/acceptor | |||
Binding site | 166 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | lactoylglutathione lyase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLactoylglutathione lyase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A2D2M7T4
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length173
- Mass (Da)19,617
- Last updated2018-01-31 v1
- Checksum69FC8B9FED1FC342
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP024478 EMBL· GenBank· DDBJ | ATR83578.1 EMBL· GenBank· DDBJ | Genomic DNA |