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 |