The domain within your query sequence starts at position 228 and ends at position 686; the E-value for the Lipoxygenase domain shown below is 5.3e-59.



PFAM accession number:PF00305
Interpro abstract (IPR013819):

Lipoxygenases ([intenz: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:metal ion binding (GO:0046872), oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (GO:0016702)

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