| IED ID | IndEnz0018000903 |
| Enzyme Type ID | peroxidase000903 |
| Protein Name |
Cytochrome P450 119 EC 1.14.-.- Peroxidase EC 1.11.1.7 |
| Gene Name | cyp119 Saci_2081 |
| Organism | Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) |
| Taxonomic Lineage | cellular organisms Archaea TACK group Crenarchaeota Thermoprotei Sulfolobales Sulfolobaceae Sulfolobus Sulfolobus acidocaldarius Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) |
| Enzyme Sequence | MYDWFSEMRKKDPVYYDGNIWQVFSYRYTKEVLNNFSKFSSDLTGYHERLEDLRNGKIRFDIPTRYTMLTSDPPLHDELRSMSADIFSPQKLQTLETFIRETTRSLLDSIDPREDDIVKKLAVPLPIIVISKILGLPIEDKEKFKEWSDLVAFRLGKPGEIFELGKKYLELIGYVKDHLNSGTEVVSRVVNSNLSDIEKLGYIILLLIAGNETTTNLISNSVIDFTRFNLWQRIREENLYLKAIEEALRYSPPVMRTVRKTKERVKLGDQTIEEGEYVRVWIASANRDEEVFHDGEKFIPDRNPNPHLSFGSGIHLCLGAPLARLEARIAIEEFSKRFRHIEILDTEKVPNEVLNGYKRLVVRLKSNE |
| Enzyme Length | 368 |
| Uniprot Accession Number | Q55080 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 76; /note="Heme"; /evidence="ECO:0000269|PubMed:10859321, ECO:0000269|PubMed:10957637"; BINDING 80; /note="Heme"; /evidence="ECO:0000269|PubMed:10859321, ECO:0000269|PubMed:10957637"; BINDING 257; /note="Heme"; /evidence="ECO:0000269|PubMed:10859321, ECO:0000269|PubMed:10957637"; BINDING 259; /note="Heme"; /evidence="ECO:0000269|PubMed:10859321, ECO:0000269|PubMed:10957637"; BINDING 315; /note="Heme"; /evidence="ECO:0000269|PubMed:10859321, ECO:0000269|PubMed:10957637" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; |
| DNA Binding | |
| EC Number | 1.14.-.-; 1.11.1.7 |
| Enzyme Function | FUNCTION: The endogenous substrate is not known. In vitro, catalyzes the H(2)O(2)-dependent epoxidation of styrene, cis-beta-methylstyrene, and cis-stilbene with retention of stereochemistry. Is able to use cumene hydroperoxide (CHP) or tert-butyl hydroperoxide (TBHP) instead of H(2)O(2) as the electron acceptor. Can also hydroxylate fatty acids such as lauric acid. {ECO:0000269|PubMed:10799487, ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 75 degrees Celsius. Activity is 10-fold greater at 75 degrees Celsius than that measured at 25 degrees Celsius. Thermostable up to 85 degrees Celsius. Thermal denaturation midpoint (Tm) is 91 degrees Celsius. {ECO:0000269|PubMed:10799487, ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for peroxidase activity. {ECO:0000269|PubMed:10799487, ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (12); Binding site (5); Chain (1); Helix (23); Metal binding (1); Mutagenesis (8); Turn (6) |
| Keywords | 3D-structure;Cytoplasm;Heme;Iron;Metal-binding;Monooxygenase;Oxidoreductase;Peroxidase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (10) |
| Cross Reference PDB | 1F4T; 1F4U; 1IO7; 1IO8; 1IO9; 4TT5; 4TUV; 4WPD; 4WQJ; 5BV5; |
| Mapped Pubmed ID | 12237217; 26299431; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,863 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for lauric acid {ECO:0000269|PubMed:10799487, ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853}; KM=9.2 mM for styrene {ECO:0000269|PubMed:10799487, ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853}; |
| Metal Binding | METAL 317; /note=Iron (heme axial ligand) |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda | 1.11.1.7; |