A0A1B7YPJ0 · A0A1B7YPJ0_COLHI
- ProteinGlutathione synthetase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids536 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- gamma-L-glutamyl-L-cysteine + glycine + ATP = glutathione + ADP + phosphate + H+
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 153 | substrate | ||||
Sequence: R | ||||||
Binding site | 175 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 175 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 177 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 179-182 | substrate | ||||
Sequence: IASS | ||||||
Binding site | 255-257 | substrate | ||||
Sequence: ERN | ||||||
Binding site | 261 | substrate | ||||
Sequence: Q | ||||||
Binding site | 320-323 | substrate | ||||
Sequence: RCWY | ||||||
Binding site | 359 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 426-435 | ATP (UniProtKB | ChEBI) | ||||
Sequence: KPQREGGGNN | ||||||
Binding site | 430 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 437 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 459-462 | ATP (UniProtKB | ChEBI) | ||||
Sequence: MELI | ||||||
Binding site | 485 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 512 | substrate | ||||
Sequence: R | ||||||
Binding site | 514 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 520 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 523-524 | substrate | ||||
Sequence: VA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | glutathione binding | |
Molecular Function | glutathione synthase activity | |
Molecular Function | magnesium ion binding |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione synthetase
- EC number
- Short namesGSH-S
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Glomerellaceae > Colletotrichum > Colletotrichum destructivum species complex
Accessions
- Primary accessionA0A1B7YPJ0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 246-356 | Glutathione synthase substrate-binding | ||||
Sequence: CVIFVVQGGERNIFDQRHLEYALASSPDDPVPVFRIPCSELLQHTEVAATPKRQLLYKLPRDPSKVFEVAVAYLRCWYDPSDYPDESAWEARYHLEKSAAVKCPTVLTQLA |
Sequence similarities
Belongs to the eukaryotic GSH synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length536
- Mass (Da)59,185
- Last updated2016-11-02 v1
- Checksum01B3316E15822930
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LTAN01000002 EMBL· GenBank· DDBJ | OBR13939.1 EMBL· GenBank· DDBJ | Genomic DNA |