Q9SQJ4 · Q9SQJ4_BRACM
- Proteinthioredoxin-dependent peroxiredoxin
- GeneC2C-Prx
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids273 (go to sequence)
- Protein existenceEvidence at transcript level
- 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. May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf.
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
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | thioredoxin-dependent peroxiredoxin activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namethioredoxin-dependent peroxiredoxin
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica
Accessions
- Primary accessionQ9SQJ4
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 21-42 | Disordered | ||||
Sequence: TKSSLLPSPSLSFLPTLSSPSP | ||||||
Domain | 75-239 | Thioredoxin | ||||
Sequence: PLVGNKAPDFEAEGVFDQEFIKFIKVKLSDYIGKKYVILFFLPLDFTFVCPTEITAFSDRYAEFEKLNTEVLGVSVDSVSVFSHLAGVQTDRKFGGLGDLNYPLISDVTKSISKSFGVLIHDQGIALRGLFIIDKEGVIQHSTIXNLGIGRSVDETMRTLQALQY |
Sequence similarities
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length273
- Mass (Da)29,395
- Last updated2000-05-01 v1
- Checksum0F259ECD274D1C06