Detail Information for IndEnz0018000260
IED ID IndEnz0018000260
Enzyme Type ID peroxidase000260
Protein Name 2-Cys peroxiredoxin BAS1, chloroplastic
2-Cys Prx A
2-Cys peroxiredoxin A
EC 1.11.1.24
Thiol-specific antioxidant protein A
Thioredoxin-dependent peroxiredoxin BAS1
Gene Name BAS1 At3g11630 F24K9.28 T19F11.3
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MASVASSTTLISSPSSRVFPAKSSLSSPSVSFLRTLSSPSASASLRSGFARRSSLSSTSRRSFAVKAQADDLPLVGNKAPDFEAEAVFDQEFIKVKLSDYIGKKYVILFFYPLDFTFVCPTEITAFSDRHSEFEKLNTEVLGVSVDSVFSHLAWVQTDRKSGGLGDLNYPLISDVTKSISKSFGVLIHDQGIALRGLFIIDKEGVIQHSTINNLGIGRSVDETMRTLQALQYIQENPDEVCPAGWKPGEKSMKPDPKLSKEYFSAI
Enzyme Length 266
Uniprot Accession Number Q96291
Absorption
Active Site ACT_SITE 119; /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:0000269|PubMed:12084836};
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:0000269|PubMed:12084836}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (7); Chain (1); Disulfide bond (2); Domain (1); Helix (8); Region (1); Sequence conflict (12); Transit peptide (1); Turn (3)
Keywords 3D-structure;Antioxidant;Chloroplast;Disulfide bond;Oxidoreductase;Peroxidase;Plastid;Redox-active center;Reference proteome;Transit peptide
Interact With
Induction INDUCTION: Down-regulated under highly reduced cellular thiol pool conditions. Down-regulated by ascorbate. Slightly induced by oxidative stress. {ECO:0000269|PubMed:12529539}.
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:9263459}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 5ZTE;
Mapped Pubmed ID 11826309; 11997378; 12777046; 12913160; 12938931; 14576160; 15028209; 15032878; 15276439; 15632145; 15773851; 15998247; 16055689; 16207701; 16606633; 16648217; 16891402; 16915352; 16916444; 16923014; 17028151; 17054949; 17163439; 17217469; 17828791; 18431481; 18493039; 18538804; 18625226; 18633119; 18650403; 20118269; 20584316; 20616155; 20706207; 21166475; 21798944; 24529374; 25448674; 26141131; 26872837; 27014325; 27717466; 28627464; 28644561; 28835225; 30076598; 30104347; 30279313; 30311601; 30833711; 31171656; 32564178;
Motif
Gene Encoded By
Mass 29,092
Kinetics
Metal Binding
Rhea ID RHEA:62620
Cross Reference Brenda