A2C3R2 · A2C3R2_PROM1
- Proteinthioredoxin-dependent peroxiredoxin
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids149 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Catalytic activity
- a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]-disulfide + H2O
CHEBI:35924 + RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3= CHEBI:30879 + RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ CHEBI:15377
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 44 | Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | thylakoid | |
Molecular Function | thioredoxin peroxidase activity | |
Biological Process | cell redox homeostasis | |
Biological Process | cellular response to oxidative stress |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namethioredoxin-dependent peroxiredoxin
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Prochlorococcaceae > Prochlorococcus
Accessions
- Primary accessionA2C3R2
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length149
- Mass (Da)16,784
- Last updated2007-02-20 v1
- ChecksumF685C918C9D40F6C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000553 EMBL· GenBank· DDBJ | ABM76122.1 EMBL· GenBank· DDBJ | Genomic DNA |