| IED ID | IndEnz0018000338 |
| Enzyme Type ID | peroxidase000338 |
| Protein Name |
Alpha-dioxygenase PIOX EC 1.13.11.92 Pathogen-induced oxygenase |
| Gene Name | PIOX Os12g0448900 LOC_Os12g26290 |
| Organism | Oryza sativa subsp. japonica (Rice) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Oryzoideae Oryzeae Oryzinae Oryza Oryza sativa (Rice) Oryza sativa subsp. japonica (Rice) |
| Enzyme Sequence | MGSGLFKPRVHPDLRDVFSKMSFFDKIGFLFIHAFDKRNLWHKVPVPIGLLYLNTRRTLLEKYNLLAVGRSSHGALFDPKEFLYRTEDGKYNDPHNAEAGSQNTFFGRNMEPVDQQDELMSPDPFVVATKLLARREYKDTGKQFNILAAAWIQFMVHDWMDHMEDTGQIGITAPKEVANECPLKSFKFHPTKELPTNSDGIKIGHYNIRTAWWDGSAVYGNNEERAEKLRTYVDGKLVIGDDGLLLHKENGVALSGDIRNSWAGVSILQALFVKEHNAVCDAIKEEHPNLSDEELYRYAKLVTSAVIAKVHTIDWTVELLKTKTMRAAMRANWYGLLGKKIKDTFGHIGGPILGGLVGLKKPNNHGVPYSLTEEFTSVYRMHSLIPSTLKLRDPTGQPDANNSPPCLEDIDIGEMIGLKGEEQLSKIGFEKQALSMGYQACGALELWNYPSFFRNLIPQNLDGTNRSDRIDLAALEVYRDRERSVPRYNEFRRRLFLIPIKSWEDLTSDKDAIETIRAIYGDDVEKLDLLVGLMAEKKIKGFAISETAFNIFILMASRRLEADRFFTSNFNEETYTKKGMQWVKTTEGLRDVINRHYPEITAKWMKSSSAFSVWDADY |
| Enzyme Length | 618 |
| Uniprot Accession Number | Q2QRV3 |
| Absorption | |
| Active Site | ACT_SITE 157; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | BINDING 162; /note=Heme b; /evidence=ECO:0000269|PubMed:23934749; BINDING 311; /note=Hexadecanoate; /evidence=ECO:0000269|PubMed:23934749; BINDING 479; /note=Heme b; /evidence=ECO:0000269|PubMed:23934749; BINDING 483; /note=Heme b; /evidence=ECO:0000269|PubMed:23934749; BINDING 599; /note=Hexadecanoate; /evidence=ECO:0000269|PubMed:23934749 |
| 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:11909851, ECO:0000269|PubMed:18596034};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63509; Evidence={ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034}; 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:11909851, ECO:0000269|PubMed:18596034};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63861; Evidence={ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034}; 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:11909851, ECO:0000269|PubMed:18596034};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63837; Evidence={ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034}; 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:18596034};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16330; Evidence={ECO:0000269|PubMed:18596034}; CATALYTIC ACTIVITY: Reaction=O2 + tetradecanoate = (2R)-2-hydroperoxytetradecanoate; Xref=Rhea:RHEA:63856, ChEBI:CHEBI:15379, ChEBI:CHEBI:30807, ChEBI:CHEBI:149617; EC=1.13.11.92; Evidence={ECO:0000269|PubMed:18596034};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63857; Evidence={ECO:0000269|PubMed:18596034}; CATALYTIC ACTIVITY: Reaction=O2 + octadecanoate = (2R)-2-hydroperoxyoctadecanoate; Xref=Rhea:RHEA:63864, ChEBI:CHEBI:15379, ChEBI:CHEBI:25629, ChEBI:CHEBI:149622; EC=1.13.11.92; Evidence={ECO:0000269|PubMed:18596034};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63865; Evidence={ECO:0000269|PubMed:18596034}; 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:18596034};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63869; Evidence={ECO:0000269|PubMed:18596034}; |
| 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:11909851, PubMed:18596034). Involved in the production of oxylipins that function in cell signaling, wound healing, and protection from infection (PubMed:11909851, PubMed:18596034). {ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (5); Chain (1); Metal binding (6); Mutagenesis (15); Site (1) |
| Keywords | 3D-structure;Calcium;Dioxygenase;Fatty acid biosynthesis;Fatty acid metabolism;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Metal-binding;Oxidoreductase;Oxylipin biosynthesis;Peroxidase;Plant defense;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 4KVJ; 4KVK; 4KVL; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 70,441 |
| Kinetics | |
| Metal Binding | METAL 158; /note="Calcium"; /evidence="ECO:0000269|PubMed:23934749"; METAL 210; /note="Calcium"; /evidence="ECO:0000269|PubMed:23934749"; METAL 212; /note="Calcium"; /evidence="ECO:0000269|PubMed:23934749"; METAL 214; /note="Calcium"; /evidence="ECO:0000269|PubMed:23934749"; METAL 216; /note="Calcium"; /evidence="ECO:0000269|PubMed:23934749"; METAL 382; /note="Iron (heme b axial ligand)"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:23934749" |
| Rhea ID | RHEA:63508; RHEA:63509; RHEA:63860; RHEA:63861; RHEA:63836; RHEA:63837; RHEA:16329; RHEA:16330; RHEA:63856; RHEA:63857; RHEA:63864; RHEA:63865; RHEA:63868; RHEA:63869 |
| Cross Reference Brenda |