Detail Information for IndEnz0018001664
IED ID IndEnz0018001664
Enzyme Type ID peroxidase001664
Protein Name Peroxiredoxin Q, chloroplastic
EC 1.11.1.24
Thioredoxin peroxidase
Thioredoxin-dependent peroxiredoxin Q
Gene Name PRXQ At3g26060 MPE11_21
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 MAASSSSFTLCNHTTLRTLPLRKTLVTKTQFSVPTKSSESNFFGSTLTHSSYISPVSSSSLKGLIFAKVNKGQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYKLPYTLLSDEGNKVRKDWGVPGDLFGALPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKAA
Enzyme Length 216
Uniprot Accession Number Q9LU86
Absorption
Active Site ACT_SITE 111; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P0AE52
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:21798375};
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. Involved in the photosystem II protection against hydrogen peroxide. {ECO:0000269|PubMed:12084836, ECO:0000269|PubMed:16507087, ECO:0000269|PubMed:21798375}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:21798375};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:21798375};
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (1); Domain (1); Transit peptide (2)
Keywords Alternative splicing;Antioxidant;Chloroplast;Direct protein sequencing;Disulfide bond;Oxidoreductase;Peroxidase;Plastid;Redox-active center;Reference proteome;Thylakoid;Transit peptide
Interact With P0AA25; P07591
Induction INDUCTION: Highly induced by oxidative stress. Down-regulated by salt stress and by ascorbate. {ECO:0000269|PubMed:12529539, ECO:0000269|Ref.6}.
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:16507087}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11553771; 20049866;
Motif
Gene Encoded By
Mass 23,678
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=254 uM for H(2)O(2) {ECO:0000269|PubMed:21798375}; KM=1.09 uM for thioredoxin {ECO:0000269|PubMed:21798375}; Note=kcat is 4.5 sec(-1) for H(2)O(2). kcat is 2.75 sec(-1) for thioredoxin.;
Metal Binding
Rhea ID RHEA:62620
Cross Reference Brenda