Q9SRZ4 · PRX2C_ARATH
- ProteinPeroxiredoxin-2C
- GenePRXIIC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids162 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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.
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.
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
Kinetics
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
8.9 nmol/min/mg | for H2O2 |
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 51 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | thioredoxin peroxidase activity | |
Biological Process | cellular response to oxidative stress |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeroxiredoxin-2C
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9SRZ4
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000282280 | 1-162 | Peroxiredoxin-2C | |||
Sequence: MAPITVGDVVPDGTISFFDENDQLQTVSVHSIAAGKKVILFGVPGAFTPTCSMSHVPGFIGKAEELKSKGIDEIICFSVNDPFVMKAWGKTYPENKHVKFVADGSGEYTHLLGLELDLKDKGLGIRSRRFALLLDNLKVTVANVESGGEFTVSSAEDILKAL |
Proteomic databases
Expression
Tissue specificity
Highly expressed in buds and flowers. Slightly expressed in green tissues. Also detected in pollen.
Induction
Highly induced by salt or oxidative stresses.
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-162 | Thioredoxin | ||||
Sequence: ITVGDVVPDGTISFFDENDQLQTVSVHSIAAGKKVILFGVPGAFTPTCSMSHVPGFIGKAEELKSKGIDEIICFSVNDPFVMKAWGKTYPENKHVKFVADGSGEYTHLLGLELDLKDKGLGIRSRRFALLLDNLKVTVANVESGGEFTVSSAEDILKAL |
Sequence similarities
Belongs to the peroxiredoxin family. Prx5 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length162
- Mass (Da)17,414
- Last updated2000-05-01 v1
- Checksum7EEBEA0B56666E0A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF121356 EMBL· GenBank· DDBJ | AAD28243.1 EMBL· GenBank· DDBJ | mRNA | ||
AC009513 EMBL· GenBank· DDBJ | AAF06057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE34446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF332463 EMBL· GenBank· DDBJ | AAG48826.1 EMBL· GenBank· DDBJ | mRNA | ||
BT003050 EMBL· GenBank· DDBJ | AAO23615.1 EMBL· GenBank· DDBJ | mRNA | ||
AY084458 EMBL· GenBank· DDBJ | AAM61030.1 EMBL· GenBank· DDBJ | mRNA | ||
AK227350 EMBL· GenBank· DDBJ | BAE99360.1 EMBL· GenBank· DDBJ | mRNA |