| IED ID | IndEnz0018000792 |
| Enzyme Type ID | peroxidase000792 |
| Protein Name |
Alpha-dioxygenase PIOX EC 1.13.11.92 Pathogen-induced oxygenase |
| Gene Name | PIOX LOC107791409 |
| Organism | Nicotiana tabacum (Common tobacco) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Nicotianoideae Nicotianeae Nicotiana Nicotiana tabacum (Common tobacco) |
| Enzyme Sequence | MSLVMDSLKNLLLSPLRGFIHKDFHDIFERMTLLSKLLFLIVHLVDKLNLWHRLPVLLGLLYLGARRHLHQEYNLINVGKTPIGVRSNPADHPYRTADGKYNDPFNEGAGSELSFFGRNMLPVDQHNQLKKPDPMVVATKLLARRNFVDTGKQFNMIAASWIQFMIHDWIDHLEDTKQIELKAAEEVASQCPLKSFKFFKTKEIPTGFYEIKTGHLNTRTPWWDGSAIYGSNAEVLKKVRTFKDGKLKLSADGLLEIDKNGKIISGDVRNTWAGLSALQALFVQEHNSVCDALKKEYPELEEEDLYRHARLVTSAVIAKVHTIDWTVELLKTDTLLAGMRANWYGLLGKKFKDTFGHVGGSILGGFVGMKKPENYGVPYSLTEEFTSVYRMHQLLPDKLQLRNIDATPGPNKSLPLTNEIPLEDLIGGKGEENLSKIGFTKQMVSMGHQACGALELWNYPVWMRDLIPQDVDGTDRPDHIDLAALEIYRDRERSVARYNEFRRGMLQIPISKWEDLTDDEEVINTLGEVYGDDVEELDLMVGMAAEKKIKGFAISETAFFIFLVMASRRLEADRFFTSNYNEETYTKKGLEWVNTTESLKDVLDRHYPEITEKWMNSSSAFSVWDSTPQPHNPIPLYFRVPPQ |
| Enzyme Length | 643 |
| Uniprot Accession Number | A0A1S3ZX38 |
| Absorption | |
| Active Site | ACT_SITE 167; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | BINDING 172; /note=Heme b; /evidence=ECO:0000250|UniProtKB:Q9SGH6; BINDING 489; /note=Heme b; /evidence=ECO:0000250|UniProtKB:Q9SGH6; BINDING 493; /note=Heme b; /evidence=ECO:0000250|UniProtKB:Q9SGH6 |
| 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:9724698};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63509; Evidence={ECO:0000269|PubMed:9724698}; 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:9724698};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16330; Evidence={ECO:0000269|PubMed:9724698}; 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:9724698};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63861; Evidence={ECO:0000269|PubMed:9724698}; |
| 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:9724698). Involved in the production of oxylipins that function in cell signaling, wound healing, and protection from infection (PubMed:9724698). {ECO:0000269|PubMed:9724698}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (3); Chain (1); Metal binding (6); Sequence conflict (3); Site (1) |
| Keywords | 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 | INDUCTION: Induced by the elicitor harpin (HrpN) from Erwinia amylovora and infection with E.amylovora (PubMed:9724698). Induced by infection with the bacterial pathogens Pseudomonas syringae pv syringae and Pseudomonas syringae pv tabaci (PubMed:9724698). Induced by salicylate (SA), wounding, jasmonate (JA), paraquat and 3-amino-1,2,4-triazole (3AT) (PubMed:9724698). {ECO:0000269|PubMed:9724698}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 73,453 |
| Kinetics | |
| Metal Binding | METAL 168; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 220; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 222; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 224; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 226; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9SGH6; METAL 392; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | RHEA:63508; RHEA:63509; RHEA:16329; RHEA:16330; RHEA:63860; RHEA:63861 |
| Cross Reference Brenda |