J6ELC4 · J6ELC4_TRIAS
- ProteinGlutathione synthetase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids510 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H+ + phosphate
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 | 125 | substrate | ||||
Sequence: R | ||||||
Binding site | 143 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 143 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 145 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 147-150 | substrate | ||||
Sequence: IAAS | ||||||
Binding site | 221-223 | substrate | ||||
Sequence: ERN | ||||||
Binding site | 227 | substrate | ||||
Sequence: Q | ||||||
Binding site | 288-291 | substrate | ||||
Sequence: RAAY | ||||||
Binding site | 327 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 398-407 | ATP (UniProtKB | ChEBI) | ||||
Sequence: KPQREGGGNN | ||||||
Binding site | 402 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 409 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 431-434 | ATP (UniProtKB | ChEBI) | ||||
Sequence: MELI | ||||||
Binding site | 460 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 486 | substrate | ||||
Sequence: R | ||||||
Binding site | 488 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 494 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 497-498 | substrate | ||||
Sequence: VA |
GO annotations
Aspect | Term | |
---|---|---|
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 > Basidiomycota > Agaricomycotina > Tremellomycetes > Trichosporonales > Trichosporonaceae > Trichosporon
Accessions
- Primary accessionJ6ELC4
Proteomes
Organism-specific databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 212-324 | Glutathione synthase substrate-binding | ||||
Sequence: AVLFVVQPGERNVFDQRGLEYILSSKGVRVIRMTFAELGANARVGPEGRLFVRDLEGAQGVQGAQGKQFEIAVVYYRAAYTPDDYKSAKDWDTRVLLEKSTAIKCPSMALQLA |
Sequence similarities
Belongs to the eukaryotic GSH synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length510
- Mass (Da)55,838
- Last updated2012-10-31 v1
- Checksum316C6A31AC951A8C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ALBS01000337 EMBL· GenBank· DDBJ | EJT45064.1 EMBL· GenBank· DDBJ | Genomic DNA |