| IED ID | IndEnz0018000232 |
| Enzyme Type ID | peroxidase000232 |
| Protein Name |
Fatty-acid peroxygenase EC 1.11.2.4 Cytochrome P450 peroxygenase CYP152K6 |
| Gene Name | cypC CYP152K6 BMMGA3_06595 |
| Organism | Bacillus methanolicus (strain MGA3 / ATCC 53907) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus methanolicus Bacillus methanolicus (strain MGA3 / ATCC 53907) |
| Enzyme Sequence | MSNINQMPREEGIDSTWRLMEEGYMYILNRRHSFNSDIFETRLLGKKAICMGGKEAAEIFYDTEKFKRKDAAPNRVVQTLFGKNGVQALDGQTHKHRKEMFMSIMSPDELEKLTDITKKQWEIAVDKWEQMDKVILYEEAKEIMCRTACQWAGVPVQENEVKRLTKNLGAMFESAAAVGLKHWLGRHARNYEEIWIEELIDRVRDGKVNPPENTTLHKFSWYRDLEGNLLDTETAAVEVINILRPIVAIAIFINFIALALHHYPEEKEKLKSGDKKYSQMFVQEVRRFYPFFPFVVALVKKDFTWKGYKFEEGTLTLLDLYGTNHDPEIWKNPDVFSPDRFAKWEGSPFSFIPQGGGDYFMGHRCAGEWVTIEVMKVSLDYLTNRMDYEVPDQDLSFSMASMPSIPHSKVVIKNVKKRI |
| Enzyme Length | 419 |
| Uniprot Accession Number | I3DZK9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 61; /note=Heme; /evidence=ECO:0000269|PubMed:30119014; BINDING 68; /note=Heme; /evidence=ECO:0000269|PubMed:30119014; BINDING 94; /note=Heme; /evidence=ECO:0000269|PubMed:30119014; BINDING 98; /note=Heme; /evidence=ECO:0000269|PubMed:30119014; BINDING 244; /note=Substrate; /evidence=ECO:0000269|PubMed:30119014 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-saturated fatty acid + H2O2 = a 2-hydroxy fatty acid + H2O; Xref=Rhea:RHEA:48360, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:76176, ChEBI:CHEBI:83955; EC=1.11.2.4; Evidence={ECO:0000269|PubMed:30119014}; CATALYTIC ACTIVITY: Reaction=2,3-saturated fatty acid + H2O2 = 3-hydroxy fatty acid + H2O; Xref=Rhea:RHEA:48384, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:76928, ChEBI:CHEBI:84196; EC=1.11.2.4; Evidence={ECO:0000269|PubMed:30119014}; CATALYTIC ACTIVITY: Reaction=dodecanoate + H2O2 = 2-hydroxydodecanoate + H2O; Xref=Rhea:RHEA:57476, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:18262, ChEBI:CHEBI:141772; Evidence={ECO:0000269|PubMed:30119014}; CATALYTIC ACTIVITY: Reaction=2-hydroxydodecanoate + H2O2 = 2,3-dihydroxydodecanoate + H2O; Xref=Rhea:RHEA:57480, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:141772, ChEBI:CHEBI:141780; Evidence={ECO:0000269|PubMed:30119014}; |
| DNA Binding | |
| EC Number | 1.11.2.4 |
| Enzyme Function | FUNCTION: Fatty-acid peroxygenase that catalyzes the hydroxylation of dodecanoate with formation of 2-hydroxydodecanoate and only trace amounts of 3-hydroxydodecanoate. Cannot use hexadecanoate as substrate, and from tetradecanoate, forms only a small amount of the 2-hydroxylated form, with large amounts of substrate remaining. Can further convert 2-hydroxydodecanoate into 2,3-dihydroxydodecanoate and 2-hydroxydodec-2-enoate, the latter product likely leads to undec-1-en-1-ol via oxidative decarboxylation. Thus, this enzyme seems capable of both desaturation and decarboxylation reactions in addition to hydroxylation reactions. {ECO:0000269|PubMed:30119014}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (11); Binding site (5); Chain (1); Helix (18); Metal binding (1); Turn (7) |
| Keywords | 3D-structure;Fatty acid metabolism;Heme;Iron;Lipid metabolism;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6FYJ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,794 |
| Kinetics | |
| Metal Binding | METAL 365; /note=Iron (heme axial ligand); /evidence=ECO:0000269|PubMed:30119014 |
| Rhea ID | RHEA:48360; RHEA:48384; RHEA:57476; RHEA:57480 |
| Cross Reference Brenda |