P50107 · LGUL_YEAST
- ProteinGlyoxalase I
- GeneGLO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids326 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (PubMed:11050082, PubMed:8824231).
Can use gamma-glutamylcysteine as a substrate (PubMed:8824231).
Can use gamma-glutamylcysteine as a substrate (PubMed:8824231).
Miscellaneous
Present with 2570 molecules/cell in log phase SD medium.
Catalytic activity
- (R)-S-lactoylglutathione = glutathione + methylglyoxal
Cofactor
Note: Binds 1 zinc ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.41 mM | glutathione | |||||
1.2 mM | gamma-glutamylcysteine |
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 | 25 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: H | ||||||
Binding site | 29 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 89 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: E | ||||||
Binding site | 93 | substrate; ligand shared between dimeric partners | ||||
Sequence: N | ||||||
Binding site | 113 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 117 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: H | ||||||
Binding site | 117 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: H | ||||||
Binding site | 147-148 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: RQ | ||||||
Active site | 163 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 163 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Active site | 318 | Proton donor/acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | lactoylglutathione lyase activity | |
Molecular Function | metal ion binding | |
Biological Process | glutathione metabolic process | |
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 nameGlyoxalase I
- EC number
- Short namesGlx I
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP50107
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000168087 | 1-326 | Glyoxalase I | |||
Sequence: MSTDSTRYPIQIEKASNDPTLLLNHTCLRVKDPARTVKFYTEHFGMKLLSRKDFEEAKFSLYFLSFPKDDIPKNKNGEPDVFSAHGVLELTHNWGTEKNPDYKINNGNEEPHRGFGHICFSVSDINKTCEELESQGVKFKKRLSEGRQKDIAFALGPDGYWIELITYSREGQEYPKGSVGNKFNHTMIRIKNPTRSLEFYQNVLGMKLLRTSEHESAKFTLYFLGYGVPKTDSVFSCESVLELTHNWGTENDPNFHYHNGNSEPQGYGHICISCDDAGALCKEIEVKYGDKIQWSPKFNQGRMKNIAFLKDPDGYSIEVVPHGLIA |
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-167 | VOC 1 | ||||
Sequence: LLNHTCLRVKDPARTVKFYTEHFGMKLLSRKDFEEAKFSLYFLSFPKDDIPKNKNGEPDVFSAHGVLELTHNWGTEKNPDYKINNGNEEPHRGFGHICFSVSDINKTCEELESQGVKFKKRLSEGRQKDIAFALGPDGYWIELITY | ||||||
Domain | 182-322 | VOC 2 | ||||
Sequence: KFNHTMIRIKNPTRSLEFYQNVLGMKLLRTSEHESAKFTLYFLGYGVPKTDSVFSCESVLELTHNWGTENDPNFHYHNGNSEPQGYGHICISCDDAGALCKEIEVKYGDKIQWSPKFNQGRMKNIAFLKDPDGYSIEVVPH |
Sequence similarities
Belongs to the glyoxalase I family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length326
- Mass (Da)37,209
- Last updated1996-10-01 v1
- Checksum9726A8253F53FB2B
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 36 | in Ref. 2; CAC16163 | ||||
Sequence: T → A | ||||||
Sequence conflict | 156 | in Ref. 2; CAC16163 and 5; AA sequence | ||||
Sequence: G → D | ||||||
Sequence conflict | 322 | in Ref. 2; CAC16163 | ||||
Sequence: H → Y |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X99240 EMBL· GenBank· DDBJ | CAA67622.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ297938 EMBL· GenBank· DDBJ | CAC16163.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z49810 EMBL· GenBank· DDBJ | CAA89948.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S80483 EMBL· GenBank· DDBJ | AAB21302.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006946 EMBL· GenBank· DDBJ | DAA09895.1 EMBL· GenBank· DDBJ | Genomic DNA |