IED ID | IndEnz0018000709 |
Enzyme Type ID | peroxidase000709 |
Protein Name |
Peroxiredoxin Q, chloroplastic EC 1.11.1.24 Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin Q Fragment |
Gene Name | PRXQ |
Organism | Sedum lineare (Needle stonecrop) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae Saxifragales Crassulaceae Sedum Sedum lineare (Needle stonecrop) |
Enzyme Sequence | QTLQTSSQSQFHGLKFSHASSFKSPSAPLRKNSIFAKVTKGSTPPPFTLKDQEGRPVSLSKFKGKPVVVYFYPADETPGCTKQACAFRDSYEKFKKAGAEVVGISGDSSESHKAFAKKYKLPFTLLSDEGNKVRKEWGVPSDLFGTLPGRETYVLDKNGVVQLVYNNQFQPEKHIDETLKLLQSLK |
Enzyme Length | 186 |
Uniprot Accession Number | Q9MB35 |
Absorption | |
Active Site | ACT_SITE 80; /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:10998352}; |
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. {ECO:0000250|UniProtKB:Q9LU86}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1); Region (1); Transit peptide (1) |
Keywords | Antioxidant;Chloroplast;Disulfide bond;Oxidoreductase;Peroxidase;Plastid;Redox-active center;Thylakoid;Transit peptide |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000250|UniProtKB:Q9LU86}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 20,652 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:62620 |
Cross Reference Brenda | 1.11.1.24; |