A0A9R1CGT7 · A0A9R1CGT7_9TREE
- ProteinLactoylglutathione lyase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids143 (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
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 80 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 109 | 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 lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus gattii species complex
Accessions
- Primary accessionA0A9R1CGT7
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length143
- Mass (Da)16,143
- Last updated2023-09-13 v1
- Checksum9693841ADD5A5AD7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VHDQ01000011 EMBL· GenBank· DDBJ | KAE8539479.1 EMBL· GenBank· DDBJ | Genomic DNA |