| IED ID | IndEnz0018000394 |
| Enzyme Type ID | peroxidase000394 |
| Protein Name |
Cytochrome-c peroxidase IdrP1 EC 1.11.1.5 Iodate reductase subunit IdrP1 |
| Gene Name | idrP1 I8J34_RS03790 |
| Organism | Denitromonas sp. (strain IR12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Rhodocyclales Rhodocyclaceae Denitromonas unclassified Denitromonas Denitromonas sp. (strain IR12) |
| Enzyme Sequence | MGHIRSIRLALAVAAVCTAASAAAGDAKFPPLGPLPPVPVPADNPMTADKVALGKQLFWDNRLSGDGSTPCVSCHLPALGWGDGGAISRGYPGTKHWRNSQTIVNSAYYNKLFWAGSVTSLEAQAPSAAEGGVAGNGDRSLMEMRLRFIPEYVAAFKNVFGADWPRMTQAYAAIAAYQRTVVSDATRVPFDRWQAGDKAAMSAEAQRGYALFSGKAGCIACHNGPLASDQRFYNLGLPEHPDLAEDPLLQITHRWEQYQKGTTEDGYRHADRDKGYYYQTKNPKDIGKFRTPSLREVKYTGPYMHNGTLATLDEVVAFYNAGGGTAPGKTDKLKPLGLTEQESKDLVAFVEALSMTEPLIHDDPKLPGDYQPLATQ |
| Enzyme Length | 376 |
| Uniprot Accession Number | P0DV68 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 71; /note=Heme c 1; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 74; /note=Heme c 1; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 218; /note=Heme c 2; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 221; /note=Heme c 2; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5; Evidence={ECO:0000305|PubMed:34215855}; |
| DNA Binding | |
| EC Number | 1.11.1.5 |
| Enzyme Function | FUNCTION: Involved in iodate respiration (PubMed:34215855). May play a critical role in detoxification of inadvertent H(2)O(2) generated by the iodate reductase IdrA/IdrB (PubMed:34215855). {ECO:0000269|PubMed:34215855}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (4); Chain (1); Domain (2); Metal binding (2); Signal peptide (1) |
| Keywords | Heme;Iron;Metal-binding;Oxidoreductase;Periplasm;Repeat;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:A0A391NGM7}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,712 |
| Kinetics | |
| Metal Binding | METAL 75; /note=Iron (heme c 1 axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; METAL 222; /note=Iron (heme c 2 axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00433 |
| Rhea ID | RHEA:16581 |
| Cross Reference Brenda |