A0A0I1Z9C6 · A0A0I1Z9C6_SHISO
- ProteinHydroxyacylglutathione hydrolase
- GenegloB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- 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
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Shigella
Accessions
- Primary accessionA0A0I1Z9C6
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-165 | Metallo-beta-lactamase | ||||
Sequence: DNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLNKLSALPDDTLVCCAH |
Sequence similarities
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length251
- Mass (Da)28,420
- Last updated2015-10-14 v1
- ChecksumD1C80DA6A02F0982
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP019689 EMBL· GenBank· DDBJ | ARS06833.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CWXZ01000104 EMBL· GenBank· DDBJ | CSK92995.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CXDQ01000027 EMBL· GenBank· DDBJ | CSR53954.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAUUDD010000085 EMBL· GenBank· DDBJ | EFW7017593.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FTSV01000104 EMBL· GenBank· DDBJ | SIX95090.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FUBI01000101 EMBL· GenBank· DDBJ | SJH40460.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UDYI01000104 EMBL· GenBank· DDBJ | SRR24369.1 EMBL· GenBank· DDBJ | Genomic DNA |