| IED ID | IndEnz0018000961 |
| Enzyme Type ID | peroxidase000961 |
| Protein Name |
Alpha-dioxygenase 1 Alpha DOX1 EC 1.13.11.92 Fatty acid dioxygenase AlphaDOX1 Pathogen-induced oxygenase Plant alpha dioxygenase 1 |
| Gene Name | DOX1 DIOX1 PADOX-1 PIOX At3g01420 T13O15.6 |
| 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 | MKVITSLISSILLKFIHKDFHEIYARMSLLDRFLLLIVHGVDKMVPWHKLPVFLGLTYLEVRRHLHQQYNLLNVGQTPTGIRFDPANYPYRTADGKFNDPFNEGVGSQNSFFGRNCPPVDQKSKLRRPDPMVVATKLLGRKKFIDTGKQFNMIAASWIQFMIHDWIDHLEDTHQIELVAPKEVASKCPLSSFRFLKTKEVPTGFFEIKTGSQNIRTPWWDSSVIYGSNSKTLDRVRTYKDGKLKISEETGLLLHDEDGLAISGDIRNSWAGVSALQALFIKEHNAVCDALKDEDDDLEDEDLYRYARLVTSAVVAKIHTIDWTVQLLKTDTLLAGMRANWYGLLGKKFKDSFGHAGSSILGGVVGMKKPQNHGVPYSLTEDFTSVYRMHSLLPDQLHILDIDDVPGTNKSLPLIQEISMRDLIGRKGEETMSHIGFTKLMVSMGHQASGALELMNYPMWLRDIVPHDPNGQARPDHVDLAALEIYRDRERSVPRYNEFRRSMFMIPITKWEDLTEDEEAIEVLDDVYDGDVEELDLLVGLMAEKKIKGFAISETAFYIFLIMATRRLEADRFFTSDFNETIYTKKGLEWVNTTESLKDVIDRHYPDMTDKWMNSESAFSVWDSPPLTKNPIPLYLRIPS |
| Enzyme Length | 639 |
| Uniprot Accession Number | Q9SGH6 |
| Absorption | |
| Active Site | ACT_SITE 163; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:23373518" |
| Activity Regulation | |
| Binding Site | BINDING 168; /note=Heme b; /evidence=ECO:0000269|PubMed:23373518; BINDING 486; /note=Heme b; /evidence=ECO:0000269|PubMed:23373518; BINDING 490; /note=Heme b; /evidence=ECO:0000269|PubMed:23373518 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-saturated fatty acid + O2 = a (2R)-2-hydroperoxy fatty acid; Xref=Rhea:RHEA:63508, ChEBI:CHEBI:15379, ChEBI:CHEBI:83955, ChEBI:CHEBI:147340; EC=1.13.11.92; Evidence={ECO:0000269|PubMed:10455113};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63509; Evidence={ECO:0000269|PubMed:10455113}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (R)-2-hydroperoxy-(9Z,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:16329, ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:76161; EC=1.13.11.92; Evidence={ECO:0000269|PubMed:10455113};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16330; Evidence={ECO:0000269|PubMed:10455113}; CATALYTIC ACTIVITY: Reaction=hexadecanoate + O2 = (2R)-2-hydroperoxyhexadecanoate; Xref=Rhea:RHEA:63836, ChEBI:CHEBI:7896, ChEBI:CHEBI:15379, ChEBI:CHEBI:149616; EC=1.13.11.92; Evidence={ECO:0000269|PubMed:10455113};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63837; Evidence={ECO:0000269|PubMed:10455113}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (2R,9Z,12Z)-2-hydroperoxyoctadecadienoate; Xref=Rhea:RHEA:63860, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:149618; EC=1.13.11.92; Evidence={ECO:0000269|PubMed:10455113};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63861; Evidence={ECO:0000269|PubMed:10455113}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + O2 = (2R,9Z)-2-hydroperoxyoctadecenoate; Xref=Rhea:RHEA:63868, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823, ChEBI:CHEBI:149623; EC=1.13.11.92; Evidence={ECO:0000269|PubMed:10455113};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63869; Evidence={ECO:0000269|PubMed:10455113}; |
| DNA Binding | |
| EC Number | 1.13.11.92 |
| Enzyme Function | FUNCTION: Alpha-dioxygenase that catalyzes the primary oxygenation step of a variety of 14-20 carbon fatty acids, containing up to three unsaturated bonds, into their corresponding 2R-hydroperoxides (PubMed:12060227, PubMed:10455113). Involved in the production of oxylipins that function in cell signaling, wound healing, and protection from infection (PubMed:12060227, PubMed:10455113). Mediates protection against oxidative stress and cell death, probably by generating some lipid-derived molecules (PubMed:12060227). Promotes local and systemic plant defense in a salicylic acid (SA)-dependent manner, including the establishment of systemic acquired resistance (SAR) in response to incompatible interaction (PubMed:22199234). Involved in a negative regulation of abscisic acid (ABA)-mediated signaling pathway (PubMed:22199234). {ECO:0000269|PubMed:10455113, ECO:0000269|PubMed:12060227, ECO:0000269|PubMed:22199234}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Binding site (3); Chain (1); Helix (39); Metal binding (6); Mutagenesis (18); Site (1); Turn (6) |
| Keywords | 3D-structure;Dioxygenase;Fatty acid biosynthesis;Fatty acid metabolism;Heme;Hypersensitive response;Iron;Lipid biosynthesis;Lipid droplet;Lipid metabolism;Metal-binding;Oxidoreductase;Oxylipin biosynthesis;Peroxidase;Plant defense;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Induced by salicylic acid (SA) and by some chemicals generating reactive oxygen species (ROS, e.g. nitric oxide (NO), intracellular superoxide and singlet oxygen) such as sodium nitropruside (SNP), paraquat and rose bengal (RB). Accumulates locally, at the infection site, in response to both incompatible and compatible bacterial pathogens (e.g. Pseudomonas syringae pv. tomato DC3000) in a SA-dependent manner, with a faster response during hypersensitive reactions. {ECO:0000269|PubMed:12060227}. |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:24214535}. Note=Localizes on the surface of leaf oil bodies. {ECO:0000269|PubMed:24214535}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4HHR; 4HHS; |
| Mapped Pubmed ID | 12376638; 14996219; 15235117; 15272873; 15319476; 15824099; 15860015; 15911562; 16262716; 16307367; 16581873; 16889973; 17149585; 17704230; 18326828; 18650403; 18772308; 19759339; 20736450; 23148892; 23487466; 23505340; 23858430; 27247031; 29119291; |
| Motif | |
| Gene Encoded By | |
| Mass | 73,158 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for linolenic acid (at pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:10455113}; KM=17 uM for linoleic acid (at pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:10455113}; KM=13 uM for oleic acid (at pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:10455113}; KM=14 uM for oleic acid (at pH 7.8 and 30 degrees Celsius) {ECO:0000269|PubMed:15100225}; KM=11 uM for palmitic acid (at pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:10455113}; Vmax=119 nmol/min/mg enzyme with linolenic acid as substrate (at pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:10455113}; Vmax=111 nmol/min/mg enzyme with linoleic acid as substrate (at pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:10455113}; Vmax=91 nmol/min/mg enzyme with oleic acid as substrate (at pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:10455113}; Vmax=46 nmol/min/mg enzyme with palmitic acid as substrate (at pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:10455113}; |
| Metal Binding | METAL 164; /note="Calcium"; /evidence="ECO:0000269|PubMed:23373518"; METAL 216; /note="Calcium"; /evidence="ECO:0000269|PubMed:23373518"; METAL 218; /note="Calcium"; /evidence="ECO:0000269|PubMed:23373518"; METAL 220; /note="Calcium"; /evidence="ECO:0000269|PubMed:23373518"; METAL 222; /note="Calcium"; /evidence="ECO:0000269|PubMed:23373518"; METAL 389; /note="Iron (heme b axial ligand)"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:23373518" |
| Rhea ID | RHEA:63508; RHEA:63509; RHEA:16329; RHEA:16330; RHEA:63836; RHEA:63837; RHEA:63860; RHEA:63861; RHEA:63868; RHEA:63869 |
| Cross Reference Brenda |