| IED ID | IndEnz0018000339 |
| Enzyme Type ID | peroxidase000339 |
| Protein Name |
Alpha-dioxygenase PIOX EC 1.13.11.92 Pathogen-induced oxygenase |
| Gene Name | alphaDOX1 |
| Organism | Pisum sativum (Garden pea) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade Hologalegina IRL clade Fabeae Pisum Pisum sativum (Garden pea) |
| Enzyme Sequence | MWSIVTDPIKDLISKVVKNSIHPDFHDAVSKMTIIDAFLFFIVHSIDKLGIWHRLPVFFGLLYLAIRRHLHQEYNLLNVGTTPVGIRSNPSDFPYRTADGRYNDPFNDGAGSQGSFFGRNILPVDQKNKLLKPDPMVVVTKLLERKTYKDTGTQFNVIAASWIQFMIHDWIDHMEDTKQVELSAPSEVASQCPLKSFKFFKTKEIPTGFYDIKTGHANVRTPWWDGSVVYGSNEQVLNKVRTFKDGKLKISKEGHLLHNEDGTAISGDIRNSWAGVTTLQTLFVQEHNAVCDALKKENSDLEDEDLYRHARLVTSAVIAKIHTIDWTVELLKTDTLLAGMRANWYGLLGKQFKDRFGHVGNSILSGFVGMKRSENHGVPYSLTEEFATVYRMHPLLPDSLHLRDISASPGPNKSPPLIKEIPMNDLIGLQGEKTLLEIGNAKKLVSMGHQACGALELWNYPSWLRNLVPHNIDGTERSDHVDLAALEVYRDRERNVARYNQFRRGLLLIPISKWEDLTDDEEAIKVLEEVYGDDVEELDVLVGLMAEKKIKGFAISETAFVIFLLMASRRLEADRFFTSNFNEETYTKKGLEWVNTTESLKDVIDRHHPEMTHKWLNSSSAFSVWDTSPNKHNHIPIYFRVPN |
| Enzyme Length | 643 |
| Uniprot Accession Number | Q5GQ66 |
| Absorption | |
| Active Site | ACT_SITE 168; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | BINDING 173; /note=Heme b; /evidence=ECO:0000250|UniProtKB:Q9SGH6; BINDING 490; /note=Heme b; /evidence=ECO:0000250|UniProtKB:Q9SGH6; BINDING 494; /note=Heme b; /evidence=ECO:0000250|UniProtKB:Q9SGH6 |
| Calcium Binding | |
| catalytic Activity | 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:10938370};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63837; Evidence={ECO:0000269|PubMed:10938370}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 = (2R)-2-hydroperoxydodecanoate; Xref=Rhea:RHEA:63852, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:149611; EC=1.13.11.92; Evidence={ECO:0000269|PubMed:10938370};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63853; Evidence={ECO:0000269|PubMed:10938370}; |
| 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:18760499, PubMed:10938370). Involved in the production of oxylipins that function in cell signaling, wound healing, and protection from infection (PubMed:18760499, PubMed:10938370). The alpha-oxidation pathway of fatty acids may play a role during plant developmental processes (PubMed:18760499). {ECO:0000269|PubMed:10938370, ECO:0000269|PubMed:18760499}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (3); Chain (1); Metal binding (6); Site (1) |
| Keywords | Calcium;Dioxygenase;Direct protein sequencing;Fatty acid biosynthesis;Fatty acid metabolism;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Metal-binding;Oxidoreductase;Oxylipin biosynthesis;Peroxidase;Plant defense |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 73,297 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 uM for O2 {ECO:0000269|PubMed:10938370}; KM=55 uM for dodecanoate {ECO:0000269|PubMed:10938370}; |
| Metal Binding | METAL 169; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 221; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 223; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 225; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 227; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 393; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | RHEA:63836; RHEA:63837; RHEA:63852; RHEA:63853 |
| Cross Reference Brenda |