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; |