The domain within your query sequence starts at position 163 and ends at position 662; the E-value for the Lipoxygenase domain shown below is 5.5e-70.



PFAM accession number:PF00305
Interpro abstract (IPR013819):

Lipoxygenases (EC 1.13.11.-) are a class of iron-containing dioxygenases which catalyses the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure. They are common in plants where they may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. In mammals a number of lipoxygenases isozymes are involved in the metabolism of prostaglandins and leukotrienes [(PUBMED:3017195)]. Sequence data is available for the following lipoxygenases:

  • Plant lipoxygenases (EC Plants express a variety of cytosolic isozymes as well as what seems to be a chloroplast isozyme [(PUBMED:7508918)].
  • Mammalian arachidonate 5-lipoxygenase (EC
  • Mammalian arachidonate 12-lipoxygenase (EC
  • Mammalian arachidonate 15-lipoxygenase B (also known as erythroid cell-specific 15-lipoxygenase; EC

The iron atom in lipoxygenases is bound by four ligands, three of which are histidine residues [(PUBMED:8502991)]. Six histidines are conserved in all lipoxygenase sequences, five of them are found clustered in a stretch of 40 amino acids. This region contains two of the three iron-ligands; the other histidines have been shown [(PUBMED:1567851)] to be important for the activity of lipoxygenases.

This entry represents the C-terminal region of these proteins.

GO process:oxidation-reduction process (GO:0055114)
GO function:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (GO:0016702), metal ion binding (GO:0046872)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Lipoxygenase