Q9SDD6 · PRX2F_ORYSJ
- ProteinPeroxiredoxin-2F, mitochondrial
- GenePRXIIF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids198 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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. Reduces preferentially hydrogen peroxide rather than alkyl peroxides. May be involved in mitochondrial redox homeostasis.
Miscellaneous
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule. C(P) can be reactivated by glutathione or the mitochondrial glutaredoxin (Grx) or thioredoxin (Trx) systems.
Catalytic activity
- [glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-disulfide + an alcohol + H2O
RHEA-COMP:10729 CHEBI:29950 Position: nCHEBI:29950 Position: n+3+ CHEBI:35924 = RHEA-COMP:10730 CHEBI:50058 Position: n/n+3+ CHEBI:30879 + CHEBI:15377
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 86 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | thioredoxin peroxidase activity | |
Biological Process | cell redox homeostasis | |
Biological Process | cellular response to oxidative stress | |
Biological Process | hydrogen peroxide catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeroxiredoxin-2F, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ9SDD6
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-27 | Mitochondrion | ||||
Sequence: MASALLRKATVGGSAAAAAARWASRGL | ||||||
Chain | PRO_0000282962 | 28-198 | Peroxiredoxin-2F, mitochondrial | |||
Sequence: ASVGSGSDIVSAAPGVSLQKARSWDEGVATNFSTTPLKDIFHGKKVVIFGLPGAYTGVCSQAHVPSYKNNIDKLKAKGVDSVICVSVNDPYALNGWAEKLQAKDAIEFYGDFDGSFHKSLDLEVDLSAALLGRRSHRWSAFVDDGKIKAFNVEVAPSDFKVSGAEVILDQI |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-198 | Thioredoxin | ||||
Sequence: SDIVSAAPGVSLQKARSWDEGVATNFSTTPLKDIFHGKKVVIFGLPGAYTGVCSQAHVPSYKNNIDKLKAKGVDSVICVSVNDPYALNGWAEKLQAKDAIEFYGDFDGSFHKSLDLEVDLSAALLGRRSHRWSAFVDDGKIKAFNVEVAPSDFKVSGAEVILDQI |
Sequence similarities
Belongs to the peroxiredoxin family. Prx5 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length198
- Mass (Da)20,874
- Last updated2000-05-01 v1
- Checksum21362AB6D2964CCD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP000969 EMBL· GenBank· DDBJ | BAA88530.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP001080 EMBL· GenBank· DDBJ | BAA90363.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008207 EMBL· GenBank· DDBJ | BAF04594.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014957 EMBL· GenBank· DDBJ | BAS71469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK058396 EMBL· GenBank· DDBJ | BAG86680.1 EMBL· GenBank· DDBJ | mRNA |