A0A0M9G2B3 · A0A0M9G2B3_LEPPY
- ProteinTrypanothione reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids491 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
Catalytic activity
- trypanothione + NADP+ = trypanothione disulfide + NADPH + H+
Cofactor
Note: Binds 1 FAD per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 61 | FAD (UniProtKB | ChEBI) | |||
Binding site | 127 | FAD (UniProtKB | ChEBI) | |||
Binding site | 160-162 | FAD (UniProtKB | ChEBI) | |||
Binding site | 195-202 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 286 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 327 | FAD (UniProtKB | ChEBI) | |||
Active site | 461 | Proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | glutathione-disulfide reductase (NADPH) activity | |
Molecular Function | trypanothione-disulfide reductase (NADPH) activity | |
Biological Process | cell redox homeostasis | |
Biological Process | cellular response to oxidative stress | |
Biological Process | glutathione metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTrypanothione reductase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leptomonas
Accessions
- Primary accessionA0A0M9G2B3
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Disulfide bond | 52↔57 | Redox-active | |||
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 5-342 | FAD/NAD(P)-binding | |||
Domain | 363-468 | Pyridine nucleotide-disulphide oxidoreductase dimerisation | |||
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length491
- Mass (Da)53,101
- Last updated2015-12-09 v1
- MD5 ChecksumF58AEFF41417E1841998F2BD01DA32E0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LGTL01000007 EMBL· GenBank· DDBJ | KPA80793.1 EMBL· GenBank· DDBJ | Genomic DNA |