| IED ID | IndEnz0018000825 |
| Enzyme Type ID | peroxidase000825 |
| Protein Name |
Cytochrome-c peroxidase IdrP1 EC 1.11.1.5 Iodate reductase subunit IdrP1 |
| Gene Name | idrP1 PSCT_04483 |
| Organism | Pseudomonas sp. (strain SCT) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas unclassified Pseudomonas Pseudomonas sp. (strain SCT) |
| Enzyme Sequence | MNNRKPLQLSLLVASLAVAFTASATNADAHPPLAPLPPVPVPKDNPQSAEKIALGKQLFWDYRLSGDGSMPCVSCHLPALGWGDGGQISRGYPGTKHWRNSQTILNSAYYNKLFWEGSVNSLEEQAPSAAEGAVAGNGDPSVMEMRLRFVPEYVDAFKNVFGSQWPRMNDAYRAIASYQRTVVSDASKVPFDRYANGDKNALDTSQKRGMALFNGKAGCVQCHNGPLASDQKYYDLGLPDFAGFVDDPLYQVTHRWEHYQKGVSEPRYRAANMDYGLYYVTKNPKDVGKFRTPSLREAKYTAPYMHNGVFTSLQEVVDFYDRGGGSGTSKSELLKPLKLAAQEKQDLIAFIEALSMSEPLLHDDPTLPGEYQPLPAPIK |
| Enzyme Length | 379 |
| Uniprot Accession Number | A0A391NGM7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 72; /note=Heme c 1; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 75; /note=Heme c 1; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 219; /note=Heme c 2; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 222; /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:32190953}; |
| DNA Binding | |
| EC Number | 1.11.1.5 |
| Enzyme Function | FUNCTION: Involved in iodate respiration (PubMed:32190953). Probably reduces the H(2)O(2) produced by IdrA/IdrB to H(2)O, using a reduced cytochrome c as the electron donor (PubMed:32190953). {ECO:0000269|PubMed:32190953}. |
| 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 | INDUCTION: Abundantly expressed under iodate-respiring conditions. {ECO:0000269|PubMed:32190953}. |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:32190953}. |
| 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 | 41,822 |
| Kinetics | |
| Metal Binding | METAL 76; /note=Iron (heme c 1 axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; METAL 223; /note=Iron (heme c 2 axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00433 |
| Rhea ID | RHEA:16581 |
| Cross Reference Brenda |