X5DNM4 · X5DNM4_HUMAN
- ProteinLactoylglutathione lyase
- GeneGLO1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids184 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic activity
- (R)-S-lactoylglutathione = glutathione + methylglyoxal
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, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 34 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: Q | ||||||
Binding site | 34 | substrate; ligand shared between dimeric partners | ||||
Sequence: Q | ||||||
Binding site | 38 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 100 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: E | ||||||
Binding site | 104 | substrate; ligand shared between dimeric partners | ||||
Sequence: N | ||||||
Binding site | 123 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 127 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: H | ||||||
Binding site | 127 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: H | ||||||
Binding site | 157-158 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: KM | ||||||
Active site | 173 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 173 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | lactoylglutathione lyase activity | |
Molecular Function | zinc ion binding | |
Biological Process | glutathione metabolic process | |
Biological Process | methylglyoxal metabolic process | |
Biological Process | osteoclast differentiation | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLactoylglutathione lyase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionX5DNM4
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Organism-specific databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-177 | VOC | ||||
Sequence: LLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNP |
Sequence similarities
Belongs to the glyoxalase I family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length184
- Mass (Da)20,778
- Last updated2014-06-11 v1
- Checksum46291B7878070028
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 184 | |||||
Sequence: M |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KJ534846 EMBL· GenBank· DDBJ | AHW56486.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471081 EMBL· GenBank· DDBJ | EAX03964.1 EMBL· GenBank· DDBJ | Genomic DNA |