| IED ID | IndEnz0018000809 |
| Enzyme Type ID | peroxidase000809 |
| Protein Name |
Iodotyrosine deiodinase EC 1.21.1.1 Halotyrosine dehalogenase Protein condet |
| Gene Name | Iyd cdt CG46438 |
| 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 | MDVDELISSSKLLKHWPSLFITLALIWIVKRLFFKGNRVLKTYNLDEQVEEEVEHFADLGDELQPALEDKPHVPFVPGQNLNPNGAKRLYELMRGRRSIRSFNSHPKPDLSVIEDCIRAAGTAPSGAHTEPWTYCVVQEPELKRSIREIVEQEELVNYSQRMHPQWVTDLRPLQTNHVKEYLTEAPYLILIFKQTYGLSENGKRMRRHYYNEISTSIAAGILLCALQAAGLASLVTTPLNCGPALRNLLGRPVNEKLLILLPVGYPKDGCTVPDLARKNLSNIMVTF |
| Enzyme Length | 287 |
| Uniprot Accession Number | E1JIB2 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 125; /note="FMN; via amide nitrogen"; /evidence="ECO:0000250|UniProtKB:Q6PHW0"; BINDING 127; /note="3,5-diiodo-L-tyrosine; via amide nitrogen"; /evidence="ECO:0000250|UniProtKB:Q9DCX8"; BINDING 127; /note="3-iodo-L-tyrosine; via amide nitrogen"; /evidence="ECO:0000250|UniProtKB:Q9DCX8"; BINDING 154; /note="3,5-diiodo-L-tyrosine"; /evidence="ECO:0000269|PubMed:27643701"; BINDING 154; /note="3-iodo-L-tyrosine"; /evidence="ECO:0000269|PubMed:27643701"; BINDING 158; /note="3,5-diiodo-L-tyrosine"; /evidence="ECO:0000269|PubMed:27643701"; BINDING 158; /note="3-iodo-L-tyrosine"; /evidence="ECO:0000269|PubMed:27643701"; BINDING 179; /note="3,5-diiodo-L-tyrosine"; /evidence="ECO:0000269|PubMed:27643701"; BINDING 179; /note="3-iodo-L-tyrosine"; /evidence="ECO:0000269|PubMed:27643701"; BINDING 277; /note="FMN"; /evidence="ECO:0000250|UniProtKB:Q6PHW0" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH; Xref=Rhea:RHEA:32479, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.21.1.1; Evidence={ECO:0000269|PubMed:27643701};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32481; Evidence={ECO:0000269|PubMed:27643701}; CATALYTIC ACTIVITY: Reaction=iodide + L-tyrosine + NADP(+) = 3-iodo-L-tyrosine + NADPH; Xref=Rhea:RHEA:27453, ChEBI:CHEBI:16382, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000269|PubMed:27643701};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27455; Evidence={ECO:0000269|PubMed:27643701}; CATALYTIC ACTIVITY: Reaction=3-iodo-L-tyrosine + iodide + NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + NADPH; Xref=Rhea:RHEA:27457, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000269|PubMed:27643701};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27459; Evidence={ECO:0000269|PubMed:27643701}; CATALYTIC ACTIVITY: Reaction=chloride + L-tyrosine + NADP(+) = 3-chloro-L-tyrosine + NADPH; Xref=Rhea:RHEA:70343, ChEBI:CHEBI:17996, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189422; Evidence={ECO:0000269|PubMed:27643701};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70345; Evidence={ECO:0000269|PubMed:27643701}; CATALYTIC ACTIVITY: Reaction=bromide + L-tyrosine + NADP(+) = 3-bromo-L-tyrosine + NADPH; Xref=Rhea:RHEA:70347, ChEBI:CHEBI:15858, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189423; Evidence={ECO:0000269|PubMed:27643701};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70349; Evidence={ECO:0000269|PubMed:27643701}; |
| DNA Binding | |
| EC Number | 1.21.1.1 |
| Enzyme Function | FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (PubMed:27643701). Activity towards 3-fluoro-L-tyrosine is weak (PubMed:27643701). Important for male and female fertility (PubMed:29764939). May be involved in maintaining the viability of sperm, both during development in the testes and storage in the female spermatheca (PubMed:29764939). {ECO:0000269|PubMed:27643701, ECO:0000269|PubMed:29764939}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 96..100; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q6PHW0; NP_BIND 125..126; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q9DCX8; NP_BIND 235..237; /note=FMN; /evidence=ECO:0000250|UniProtKB:Q6PHW0 |
| Features | Binding site (10); Chain (1); Mutagenesis (3); Nucleotide binding (3); Transmembrane (1) |
| Keywords | Cell membrane;FMN;Flavoprotein;Membrane;NADP;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14668387; 20220848; 20371351; 21074052; 23071443; |
| Motif | |
| Gene Encoded By | |
| Mass | 32,597 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; KM=8 uM for 3-bromo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; KM=21 uM for 3-chloro-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; KM=11 uM for 3,5-diiodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; Note=kcat is 12 sec(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). kcat is 6.9 sec(-1) for the dehalogenation of 3-bromo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). kcat is 5.0 sec(-1) for the dehalogenation of 3-chloro-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). kcat is 10.8 sec(-1) for the dehalogenation of 3,5-diiodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). {ECO:0000269|PubMed:27643701}; |
| Metal Binding | |
| Rhea ID | RHEA:32479; RHEA:32481; RHEA:27453; RHEA:27455; RHEA:27457; RHEA:27459; RHEA:70343; RHEA:70345; RHEA:70347; RHEA:70349 |
| Cross Reference Brenda | 1.21.1.1; |