| IED ID | IndEnz0018001413 |
| Enzyme Type ID | peroxidase001413 |
| Protein Name |
Thioredoxin-1 DmTrx-1 Protein deadhead |
| Gene Name | dhd Trx-1 CG4193 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MASVRTMNDYHKRIEAADDKLIVLDFYATWCGPCKEMESTVKSLARKYSSKAVVLKIDVDKFEELTERYKVRSMPTFVFLRQNRRLASFAGADEHKLTNMMAKLVKA |
| Enzyme Length | 107 |
| Uniprot Accession Number | P47938 |
| Absorption | |
| Active Site | ACT_SITE 31; /note=Nucleophile; ACT_SITE 34; /note=Nucleophile |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. As a reducing substrate of peroxiredoxin 1, thioredoxin 2 is preferred over thioredoxin 1. Required for female meiosis and early embryonic development. {ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:9106167}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (4); Chain (1); Disulfide bond (1); Domain (1); Helix (4); Mutagenesis (2); Site (3); Turn (3) |
| Keywords | 3D-structure;Disulfide bond;Electron transport;Nucleus;Redox-active center;Reference proteome;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14579129}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6ZMU; |
| Mapped Pubmed ID | 10588726; 11158675; 11796729; 12072466; 12221129; 12408803; 12756181; 14602076; 14605208; 14630943; 15186491; 15644209; 15927177; 16313561; 16412701; 17199047; 17301052; 17567437; 17701050; 17728343; 19348653; 19543366; 20220848; 20371351; 20600005; 21074052; 21205669; 22398207; 22949888; 23071443; 23213441; 24212093; 25246242; 25761110; 25862286; 26257181; 26551273; 26801178; 26896327; 26950602; 27230753; 27486580; 27626494; 27876811; 28031247; 28428068; 29897613; 30082411; 30110626; 30294342; 30810797; 31690598; 31722958; 32134927; 32243476; 33083121; 33306674; 33708404; 34553686; 34982772; 7926776; 8878676; 9247640; 9362474; 9450931; |
| Motif | |
| Gene Encoded By | |
| Mass | 12,384 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |