A0A3L8SDR7 · A0A3L8SDR7_CHLGU
- ProteinThioredoxin reductase 1, cytoplasmic
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids528 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis. Also has reductase activity on hydrogen peroxide (H2O2).
Catalytic activity
- H2O2 + NADPH + H+ = NADP+ + 2 H2OThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 FAD per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 70 | FAD (UniProtKB | ChEBI) | |||
Binding site | 134 | FAD (UniProtKB | ChEBI) | |||
Binding site | 199-206 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 291 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 333 | FAD (UniProtKB | ChEBI) | |||
Active site | 471 | 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 | thioredoxin-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 nameThioredoxin reductase 1, cytoplasmic
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Passeroidea > Passeridae > Chloebia
Accessions
- Primary accessionA0A3L8SDR7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Disulfide bond | 61↔66 | Redox-active | |||
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 15-349 | FAD/NAD(P)-binding | |||
Domain | 369-480 | Pyridine nucleotide-disulphide oxidoreductase dimerisation | |||
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length528
- Mass (Da)57,865
- Last updated2019-02-13 v1
- ChecksumD3AE15E53F140ACC
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 528 | ||||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QUSF01000028 EMBL· GenBank· DDBJ | RLW00074.1 EMBL· GenBank· DDBJ | Genomic DNA |