LMPD Database

LMP010554

UniProt Annotations

Entry Information
Gene Namelipoxygenase 2
Protein EntryLOX2_ARATH
UniProt IDP38418
SpeciesArabidopsis
Comments
Comment typeDescription
Catalytic ActivityAlpha-linolenate + O(2) = (9Z,11E,13S,15Z)-13- hydroperoxyoctadeca-9,11,15-trienoate.
Catalytic ActivityLinoleate + O(2) = (9Z,11E,13S)-13- hydroperoxyoctadeca-9,11-dienoate.
CofactorName=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. Iron is tightly bound. {ECO:0000255|PROSITE-ProRule:PRU00726};
Developmental StageExpression is sharply reduced in leaves during leaf senescence. {ECO:0000269|PubMed:11891244}.
Function13S-lipoxygenase that can use linolenic acid as substrates. Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Required for the wound-induced synthesis of jasmonic acid (JA) in leaves. {ECO:0000269|PubMed:18949503, ECO:0000269|PubMed:7567995}.
InductionBy methyl jasmonate (MeJA) and wounding, probably through nitric oxide-mediated (NO) induction. Slightly locally induced upon herbivors infestation such as aphids (Myzus persicae and Brevicoryne brassicae), or caterpillar (Spodoptera exigua). Induced by leaf-volatiles generated by herbivors-mediated wounding such as (E)-2-hexenal, (Z)-3-hexenal, (Z)-3-hexenol or allo- ocimene (2,6-dimethyl-2,4,6-octatriene). Increased levels by bacterial pathogens (e.g. P.viridiflava and P.syringae pv. tomato). Repressed by WRKY62. {ECO:0000269|PubMed:11090221, ECO:0000269|PubMed:11161062, ECO:0000269|PubMed:11874572, ECO:0000269|PubMed:14716563, ECO:0000269|PubMed:15879447, ECO:0000269|PubMed:17313166, ECO:0000269|PubMed:17510065, ECO:0000269|PubMed:17545220, ECO:0000269|PubMed:18487634}.
InteractionO04663:EIF(ISO)4E; NbExp=7; IntAct=EBI-1770437, EBI-1770425;
PathwayLipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-ProRule:PRU00726}.
Sequence CautionSequence=CAB72152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
SimilarityBelongs to the lipoxygenase family. {ECO:0000305}.
SimilarityContains 1 lipoxygenase domain. {ECO:0000255|PROSITE- ProRule:PRU00726}.
SimilarityContains 1 PLAT domain. {ECO:0000255|PROSITE- ProRule:PRU00152}.
Subcellular LocationPlastid, chloroplast. Cytoplasm. Note=The unprocessed form is cytoplasmic whereas the cleaved form is chloroplastic.
SubunitInteracts with EIF4E2. {ECO:0000269|PubMed:11117257}.
Tissue SpecificityIn leaves and inflorescences but not abundant in seeds, roots and stems. {ECO:0000269|PubMed:17369372}.