| IED ID | IndEnz0018001128 |
| Enzyme Type ID | peroxidase001128 |
| Protein Name |
Cytochrome c551 peroxidase CCP Cytochrome c peroxidase EC 1.11.1.5 |
| Gene Name | ccpA PA4587 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MQSSQLLPLGSLLLSFATPLAQADALHDQASALFKPIPEQVTELRGQPISEQQRELGKKLFFDPRLSRSHVLSCNTCHNVGTGGADNVPTSVGHGWQKGPRNSPTVFNAVFNAAQFWDGRAKDLGEQAKGPIQNSVEMHSTPQLVEQTLGSIPEYVDAFRKAFPKAGKPVSFDNMALAIEAYEATLVTPDSPFDLYLKGDDKALDAQQKKGLKAFMDSGCSACHNGINLGGQAYFPFGLVKKPDASVLPSGDKGRFAVTKTQSDEYVFRAAPLRNVALTAPYFHSGQVWELKDAVAIMGNAQLGKQLAPDDVENIVAFLHSLSGKQPRVEYPLLPASTETTPRPAE |
| Enzyme Length | 346 |
| Uniprot Accession Number | P14532 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 74; /note=Heme c 1; covalent; /evidence=ECO:0007744|PDB:1EB7; BINDING 77; /note=Heme c 1; covalent; /evidence=ECO:0007744|PDB:1EB7; BINDING 220; /note=Heme c 2; covalent; /evidence=ECO:0007744|PDB:1EB7; BINDING 223; /note=Heme c 2; covalent; /evidence=ECO:0007744|PDB:1EB7 |
| 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:1657179}; |
| DNA Binding | |
| EC Number | 1.11.1.5 |
| Enzyme Function | FUNCTION: Catalyzes the peroxidative oxidation of azurin and cytochrome c551. Likely to provide protection against toxic peroxides. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (9); Binding site (4); Chain (1); Helix (21); Metal binding (4); Natural variant (6); Sequence conflict (10); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Direct protein sequencing;Electron transport;Heme;Iron;Metal-binding;Oxidoreductase;Periplasm;Peroxidase;Reference proteome;Signal;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Binds 2 heme groups per subunit (PubMed:8591033). Sequencing of the whole protein indicates about 20% starts on Val-247 (PubMed:8543038). {ECO:0000269|PubMed:8543038, ECO:0000269|PubMed:8591033}. |
| Signal Peptide | SIGNAL 1..23; /evidence="ECO:0000269|PubMed:2546794, ECO:0000269|PubMed:8543038" |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1EB7; 2VHD; |
| Mapped Pubmed ID | 18217775; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,403 |
| Kinetics | |
| Metal Binding | METAL 78; /note=Iron (heme c 1 axial ligand); via tele nitrogen; /evidence=ECO:0007744|PDB:1EB7; METAL 224; /note=Iron (heme c 2 axial ligand); via tele nitrogen; /evidence=ECO:0007744|PDB:1EB7; METAL 284; /note=Iron (heme c 1 axial ligand); METAL 298; /note=Iron (heme c 2 axial ligand); /evidence=ECO:0007744|PDB:1EB7 |
| Rhea ID | RHEA:16581 |
| Cross Reference Brenda | 1.11.1.5; |