Detail Information for IndEnz0018001205
IED ID IndEnz0018001205
Enzyme Type ID peroxidase001205
Protein Name 2-Cys peroxiredoxin BAS1, chloroplastic
EC 1.11.1.24
Thiol-specific antioxidant protein
Thioredoxin-dependent peroxiredoxin BAS1
Fragment
Gene Name TSA
Organism Triticum aestivum (Wheat)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Triticinae Triticum Triticum aestivum (Wheat)
Enzyme Sequence DARARSFVARAAAEYDLPLVGNKAPDFAAEAVFDQEFINVKLSDYIGKKYVILFFYPLDFTFVCPTEITAFSDRHEEFEKINTEILGVSVDSVFSHLAWVQTERKSGGLGDLKYPLVSDVTKSISKSFGVLIPDQGIALRGLFIIDKEGVIQHSTINNLGIGRSVDETLRTLRALQYVKKPDEVCPAGWKPGEKSMKPDPKGSKEYFAAI
Enzyme Length 210
Uniprot Accession Number P80602
Absorption
Active Site ACT_SITE 64; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:Q06830
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000250|UniProtKB:Q96291};
DNA Binding
EC Number 1.11.1.24
Enzyme 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. {ECO:0000250|UniProtKB:Q96291}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (2); Domain (1); Non-terminal residue (1); Transit peptide (1)
Keywords Antioxidant;Chloroplast;Direct protein sequencing;Disulfide bond;Oxidoreductase;Peroxidase;Plastid;Redox-active center;Reference proteome;Transit peptide
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250|UniProtKB:Q96291}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 23,327
Kinetics
Metal Binding
Rhea ID RHEA:62620
Cross Reference Brenda