A0A8J0QGX3 · A0A8J0QGX3_XENTR
- ProteinThioredoxin reductase 1, cytoplasmic
- Genetxnrd1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids653 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- H+ + H2O2 + NADPH = 2 H2O + NADP+This 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 | 223 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 287 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 352-359 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GASYVALE | ||||||
Binding site | 446 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 488 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 626 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | thioredoxin-disulfide reductase (NADPH) activity | |
Biological Process | cell redox homeostasis | |
Biological Process | response to oxidative stress |
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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Silurana
Accessions
- Primary accessionA0A8J0QGX3
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 214↔219 | Redox-active | ||||
Sequence: CVNVGC |
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 30-55 | Disordered | ||||
Sequence: DQSSKSPEIPKCKTNENEDNGWRTDK | ||||||
Compositional bias | 40-55 | Basic and acidic residues | ||||
Sequence: KCKTNENEDNGWRTDK | ||||||
Domain | 246-273 | PLD phosphodiesterase | ||||
Sequence: EDNIQHNWEIMTDSVLNYIGSLNFNYRV |
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length653
- Mass (Da)72,547
- Last updated2022-05-25 v1
- Checksum414D6D87FDAB5ED0
Features
Showing features for compositional bias, non-standard residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 40-55 | Basic and acidic residues | ||||
Sequence: KCKTNENEDNGWRTDK | ||||||
Non-standard residue | 652 | Selenocysteine | ||||
Sequence: U |
Keywords
- Coding sequence diversity
- Technical term