| IED ID | IndEnz0018001683 |
| Enzyme Type ID | peroxidase001683 |
| Protein Name |
Peroxiredoxin EC 1.11.1.24 Thioredoxin peroxidase ApTPx Thioredoxin-dependent peroxiredoxin |
| Gene Name | APE_2278 |
| Organism | Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) |
| Taxonomic Lineage | cellular organisms Archaea TACK group Crenarchaeota Thermoprotei Desulfurococcales Desulfurococcaceae Aeropyrum Aeropyrum pernix Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) |
| Enzyme Sequence | MPGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFSHPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYEEARTHLH |
| Enzyme Length | 250 |
| Uniprot Accession Number | Q9Y9L0 |
| Absorption | |
| Active Site | ACT_SITE 50; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649" |
| Activity Regulation | |
| Binding Site | BINDING 126; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903" |
| 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:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12707274}; |
| 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:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12707274}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (12); Binding site (1); Chain (1); Disulfide bond (3); Domain (1); Helix (10); Mutagenesis (3); Turn (4) |
| Keywords | 3D-structure;Antioxidant;Cytoplasm;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
| Interact With | Itself |
| Induction | INDUCTION: Up-regulated by hydrogen peroxide (at protein level). {ECO:0000269|PubMed:12707274}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12707274}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (21) |
| Cross Reference PDB | 1X0R; 2CV4; 2E2G; 2E2M; 2NVL; 2ZCT; 3A2V; 3A2W; 3A2X; 3A5W; 5XBS; 6KRK; 6KRM; 6KRP; 6KRQ; 6KRR; 6KRS; 7C87; 7C89; 7C8A; 7CQJ; |
| Mapped Pubmed ID | 28992240; 32022337; 33334100; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,703 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda | 1.11.1.24; |