Q9C5R8 · BAS1B_ARATH
- Protein2-Cys peroxiredoxin BAS1-like, chloroplastic
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids273 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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. May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf.
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 typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin CDSP32.
Catalytic activity
- [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O
RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3+ CHEBI:35924 = RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ CHEBI:30879 + CHEBI:15377
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 126 | Cysteine sulfenic acid (-SOH) intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apoplast | |
Cellular Component | chloroplast | |
Cellular Component | chloroplast stroma | |
Cellular Component | plasma membrane | |
Cellular Component | stromule | |
Molecular Function | peroxiredoxin activity | |
Molecular Function | thioredoxin-dependent peroxiredoxin activity | |
Biological Process | cell redox homeostasis | |
Biological Process | response to cold |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended name2-Cys peroxiredoxin BAS1-like, chloroplastic
- EC number
- Short names2-Cys Prx B; 2-Cys peroxiredoxin B
- 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 accessionQ9C5R8
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-72 | Chloroplast | ||||
Sequence: MSMASIASSSSTTLLSSSRVLLPSKSSLLSPTVSFPRIIPSSSASSSSLCSGFSSLGSLTTNRSASRRNFAV | ||||||
Chain | PRO_0000284083 | 73-273 | 2-Cys peroxiredoxin BAS1-like, chloroplastic | |||
Sequence: KAQADDLPLVGNKAPDFEAEAVFDQEFIKVKLSEYIGKKYVILFFYPLDFTFVCPTEITAFSDRYEEFEKLNTEVLGVSVDSVFSHLAWVQTDRKSGGLGDLNYPLVSDITKSISKSFGVLIPDQGIALRGLFIIDKEGVIQHSTINNLGIGRSVDETMRTLQALQYVQENPDEVCPAGWKPGEKSMKPDPKLSKEYFSAI | ||||||
Disulfide bond | 126 | Interchain (with C-248); in linked form | ||||
Sequence: C | ||||||
Disulfide bond | 248 | Interchain (with C-126); in linked form | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 80-239 | Thioredoxin | ||||
Sequence: PLVGNKAPDFEAEAVFDQEFIKVKLSEYIGKKYVILFFYPLDFTFVCPTEITAFSDRYEEFEKLNTEVLGVSVDSVFSHLAWVQTDRKSGGLGDLNYPLVSDITKSISKSFGVLIPDQGIALRGLFIIDKEGVIQHSTINNLGIGRSVDETMRTLQALQY |
Sequence similarities
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length273
- Mass (Da)29,780
- Last updated2011-05-31 v3
- Checksum33CB87338DADEB1B
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8BD74 | A0A1P8BD74_ARATH | 2-CYS | 245 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 217 | in Ref. 3; AAG40040 | ||||
Sequence: T → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB006700 EMBL· GenBank· DDBJ | BAB08951.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
CP002688 EMBL· GenBank· DDBJ | AED90999.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF324689 EMBL· GenBank· DDBJ | AAG40040.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF326871 EMBL· GenBank· DDBJ | AAG41453.1 EMBL· GenBank· DDBJ | mRNA | ||
AF339693 EMBL· GenBank· DDBJ | AAK00375.1 EMBL· GenBank· DDBJ | mRNA | ||
AY054621 EMBL· GenBank· DDBJ | AAK96812.1 EMBL· GenBank· DDBJ | mRNA | ||
AY081503 EMBL· GenBank· DDBJ | AAM10065.1 EMBL· GenBank· DDBJ | mRNA |