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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU00726


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00726
General rule information [?]

Accession PRU00726
Dates 11-JUL-2008 (Created)
19-NOV-2022 (Last updated, Version 13)
Data class Domain;
Predictors PROSITE; PS51393; LIPOXYGENASE_3
Name Lipoxygenase iron-binding catalytic domain
Function Lipoxygenases (EC 1.13.11.-) form a class of iron-containing fatty acid dioxygenases, which catalyze the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure.
Scope(s) Eukaryota
Bacteria
Example(s) Q84YK8; Q9BYJ1; Q8RNT4;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Viridiplantae>
Protein name AltName: Full=lipoxygenase;
                 EC=1.13.11.-;

Comments [?]

FUNCTIONPlant 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.
end case

Keywords [?]

Dioxygenase
case <FTGroup:1>
Iron
Metal-binding
end case
Oxidoreductase
case <OC:Viridiplantae>
Lipid metabolism
Lipid biosynthesis
Fatty acid biosynthesis
Fatty acid metabolism
Oxylipin biosynthesis
end case
case <OC:Bacteria>
Periplasm
end case

Gene Ontology [?]

GO:0016702; Molecular function:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
case <FTGroup:1>
GO:0005506; Molecular function:iron ion binding
GO:0046872; Molecular function:metal ion binding
end case
GO:0016491; Molecular function:oxidoreductase activity
case <OCellular component:Viridiplantae>
GO:0006633; Biological process:fatty acid biosynthetic process
GO:0008610; Biological process:lipid biosynthetic process
GO:0031408; Biological process:oxylipin biosynthetic process
end case
case <OCellular component:Bacteria>
GO:0042597; Cellular component:periplasmic space
end case

Cross-references [?]

PROSITE PS00711; LIPOXYGENASE_1; 1;
PROSITE PS00081; LIPOXYGENASE_2; 1;

Features [?]

From: PS51393
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Lipoxygenase #"
BINDING 340 340 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 H 1
BINDING 345 345 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 H 1
BINDING 530 530 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 H 1
BINDING 534 534 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 [NH] 1
BINDING 678 678 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 I 1

Additional information [?]

Size range 540-730 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

UniProtKB rule member sequences [?]