| IED ID | IndEnz0018000875 |
| Enzyme Type ID | peroxidase000875 |
| Protein Name |
Peroxiredoxin-5, mitochondrial EC 1.11.1.24 Alu corepressor 1 Antioxidant enzyme B166 AOEB166 Liver tissue 2D-page spot 71B PLP Peroxiredoxin V Prx-V Peroxisomal antioxidant enzyme TPx type VI Thioredoxin peroxidase PMP20 Thioredoxin-dependent peroxiredoxin 5 |
| Gene Name | PRDX5 ACR1 SBBI10 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGLAGVCALRRSAGYILVGGAGGQSAAAAARRYSEGEWASGGVRSFSRAAAAMAPIKVGDAIPAVEVFEGEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLVSIFGNRRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPNIISQL |
| Enzyme Length | 214 |
| Uniprot Accession Number | P30044 |
| Absorption | |
| Active Site | ACT_SITE 100; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000305|PubMed:10751410, ECO:0000305|PubMed:20643143" |
| 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:10751410}; |
| 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 and as sensor of hydrogen peroxide-mediated signaling events. {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410, ECO:0000269|PubMed:31740833}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (3); Beta strand (8); Chain (1); Disulfide bond (1); Domain (1); Frameshift (1); Helix (10); Lipidation (1); Modified residue (6); Motif (1); Mutagenesis (3); Natural variant (2); Sequence conflict (1); Transit peptide (1); Turn (3) |
| Keywords | 3D-structure;Acetylation;Alternative initiation;Alternative splicing;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Lipoprotein;Mitochondrion;Oxidoreductase;Palmitate;Peroxidase;Peroxisome;Phosphoprotein;Redox-active center;Reference proteome;Transit peptide |
| Interact With | P55273; Q7Z417; P49901; P00441 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410, ECO:0000269|PubMed:31740833}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic+peroxisomal]: Cytoplasm {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10751410}. Peroxisome matrix {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410}. Note=Imported into peroxisomes via peroxisomal targeting signal 1 receptor PEX5. {ECO:0000269|PubMed:10514471}. |
| Modified Residue | MOD_RES 75; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 83; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 83; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 116; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 171; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9R063; MOD_RES 182; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P99029 |
| Post Translational Modification | PTM: S-palmitoylated (PubMed:31740833). Palmitoylation occurs on the active site, inhibiting its reactivity; therefore PRDX5 palmitoylation status determines its antioxidant capacity (PubMed:31740833). {ECO:0000269|PubMed:31740833}.; PTM: [Isoform Mitochondrial]: S-palmitoylated (PubMed:31740833). Depalmitoylated by ABHD10 (PubMed:31740833). {ECO:0000269|PubMed:31740833}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (12) |
| Cross Reference PDB | 1H4O; 1HD2; 1OC3; 1URM; 2VL2; 2VL3; 2VL9; 3MNG; 4K7I; 4K7N; 4K7O; 4MMM; |
| Mapped Pubmed ID | 11717495; 11832487; 12417342; 12446202; 14732291; 14741336; 15046979; 15276323; 15280035; 15304327; 15785239; 15848167; 16169070; 16781710; 16817890; 17353931; 17519234; 17531812; 17601350; 17623739; 17628720; 17707404; 17892856; 18219526; 18262354; 18378575; 18977241; 19016754; 19336475; 19615732; 20186120; 20305821; 20596022; 20937353; 21385867; 22020876; 22304920; 23216451; 24385276; 25025339; 25525879; 25772011; 26752685; 28358580; 28431931; 28535004; 29551349; 30104402; 30391677; 30756364; 31262894; 31280208; 31375973; 31500275; 31505325; 31578139; 31861721; 31987042; 32339330; 33416106; 34888938; |
| Motif | MOTIF 212..214; /note=Microbody targeting signal; /evidence=ECO:0000305|PubMed:10514471 |
| Gene Encoded By | |
| Mass | 22,086 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda | 1.11.1.24; |