A0A0H3EF67 · A0A0H3EF67_ECO8N
- ProteinHydroxyacylglutathione hydrolase
- GenegloB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids251 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic activity
- an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H+
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 53 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 55 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 57 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 58 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 110 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 127 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 127 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 165 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | hydroxyacylglutathione hydrolase activity | |
Molecular Function | metal ion binding | |
Biological Process | methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHydroxyacylglutathione hydrolase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A0H3EF67
Proteomes
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-165 | Metallo-beta-lactamase | ||||
Sequence: DNYIWVLNDEAGRCLIVDPGDAEPVLNAISANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTPSQMYQSLKKLSALPDDTLVCCAH |
Sequence similarities
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length251
- Mass (Da)28,476
- Last updated2015-09-16 v1
- ChecksumB519BF5C36928B5A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001855 EMBL· GenBank· DDBJ | ADR25642.1 EMBL· GenBank· DDBJ | Genomic DNA |