Detail Information for IndEnz0018001374
IED ID IndEnz0018001374
Enzyme Type ID peroxidase001374
Protein Name Peroxiredoxin Q, chloroplastic
EC 1.11.1.24
Thioredoxin peroxidase
Thioredoxin-dependent peroxiredoxin Q
Gene Name AFP1
Organism Gentiana triflora (Clustered gentian)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Gentianales Gentianaceae Gentianeae Gentianinae Gentiana (gentian) Gentiana triflora (Clustered gentian)
Enzyme Sequence MAAICLPVAKHSFPSLLNTQTPKPLFSQNLHTIPLSSQSQICGLKFLISSPSSLPPPPSYSARISVFAKVSKGSVPPQFTLKDQDGKNVSLTEFKGKPVVVYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDPSSHKAFAKKYRLPYTLLSDEGNKIRREWGVPADLFGTLPGRQTYVLDKNGTVQLIYNNQFQPEKHIDETLKFLQSA
Enzyme Length 217
Uniprot Accession Number Q75SY5
Absorption
Active Site ACT_SITE 112; /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:0000250|UniProtKB:Q9LU86};
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 (By similarity). Involved in both resistance against fungal disease and oxidative stress (PubMed:15840643). {ECO:0000250|UniProtKB:Q9LU86, ECO:0000269|PubMed:15840643}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (1); Domain (1); Transit peptide (1)
Keywords Antioxidant;Chloroplast;Disulfide bond;Oxidoreductase;Peroxidase;Plastid;Redox-active center;Thylakoid;Transit peptide
Interact With
Induction INDUCTION: By salicylic acid (SA). {ECO:0000269|PubMed:15840643}.
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 23,928
Kinetics
Metal Binding
Rhea ID RHEA:62620
Cross Reference Brenda