| IED ID | IndEnz0018001133 |
| Enzyme Type ID | peroxidase001133 |
| Protein Name |
Alpha-dioxygenase 2 Alpha DOX2 EC 1.14.99.- Fatty acid dioxygenase AlphaDOX2 |
| Gene Name | DOX2 DIOX2 At1g73680 F25P22.10 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MGFSPSSSWFLHPQLHHVVSKMSYFDAFLFYIVHLVDKLGLWHRFPVLLGVAYLGLRRHLHQRYNLVHVGPINGQGYDTDEFCYRTADGKCNHPSDNTIGSQGSFIGRNMPPSTSQYGILDPHPSVVATKLLARKRFIDNGDQFNVIACSWIQFMIHDWVDHLEDTHQIELEAPEEVASGCPLKSFKFLRTKKVPTDDHHKSGAVNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLKISGDGLLERDERGVPISGDIRNSWSGFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIELLKTDTLTAGMRINWYGFFGKKVKDMVGARFGPLFSGLVGLKKPNDHGVPYSLTEEFVSVYRMHCLLPETLILRDMNSENVDKENPAIEREIPMTELIGKKAGEKASKLGFEQLLVSMGHQSCGALTLWNYPNWMRNLVAQDIDGEDRPHLIDMAALEIYRDRERGVPRYNEFRKNLLMSPISKWEELTDDEEAIKVLREVYEDDIEKLDLNVGLHAEKKIKGFAISETAFFIFLLVASRRLEADRFFTTNFNEKTYTKEGLEWVNTTETLKDVIDRHFPRLTDQWMRCSSAFSVWGSDPNPKNWVPLYLRSAP |
| Enzyme Length | 631 |
| Uniprot Accession Number | Q9C9U3 |
| Absorption | |
| Active Site | ACT_SITE 378; /note=Proton acceptor; /evidence=ECO:0000305|PubMed:19759339 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.14.99.- |
| Enzyme Function | FUNCTION: Alpha-dioxygenase that catalyzes the primary oxygenation of fatty acids into oxylipins. May be involved in the senescence process. {ECO:0000269|PubMed:19759339}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Glycosylation (1); Metal binding (2); Signal peptide (1); Site (1) |
| Keywords | Alternative splicing;Dioxygenase;Fatty acid biosynthesis;Fatty acid metabolism;Glycoprotein;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Metal-binding;Oxidoreductase;Oxylipin biosynthesis;Peroxidase;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12805597; 15047901; 15235117; 15860015; 16520461; 16581873; 17142483; 21838868; 23505340; 23858430; |
| Motif | |
| Gene Encoded By | |
| Mass | 72,458 |
| Kinetics | |
| Metal Binding | METAL 157; /note=Iron (heme b axial ligand); /evidence=ECO:0000305|PubMed:19759339; METAL 381; /note=Iron (heme b axial ligand); /evidence=ECO:0000305|PubMed:19759339 |
| Rhea ID | |
| Cross Reference Brenda |