Q42705 · Q42705_CUCSA

Function

function

Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Cofactor

Fe cation (UniProtKB | Rhea| CHEBI:24875 )

Pathway

Lipid metabolism; oxylipin biosynthesis.

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
Biological Processfatty acid biosynthetic process
Biological Processlipid oxidation
Biological Processoxylipin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipoxygenase
  • EC number

Organism names

  • Taxonomic identifier
  • Strain
    • Suyo
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Cucurbitales > Cucurbitaceae > Benincaseae > Cucumis

Accessions

  • Primary accession
    Q42705

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain57-181PLAT
Domain184-877Lipoxygenase
Region236-256Disordered

Sequence similarities

Belongs to the lipoxygenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    877
  • Mass (Da)
    99,394
  • Last updated
    1996-11-01 v1
  • Checksum
    3E173B89719FA33F
MFSIGKNIIEGALNTTGDLAGSVINAGGNIADQISNIGGQKIKGKVILMRSNVMDFTEFHSSLLDNFTELLGGGVSLQLISATQTSALDSRGKVGKKAFLERWLTSIPPLFAGESVFQVSFTWEEGFGFPGAFFIKNGHTSEFFLKSLTLEDVPGFGHVHFDCNSWVYPSGRYKKDRIFFANNTYLPSDTPNPLRKYREEELLTLRGDGTGERKEWDRIYDYDIYNDLSEPGDGRPILGGSQFPYPRRGRTGRPREWKDSNYESRLPVVSGLNIYVPRDENFGHLKLSDFLGFALKSLVATVQPALVNIVDFTPGEFDKFQDVHNLYEGGLPVPLDVFRNLTKDFTPPMFQELLRTDNDQRFLKFSPPQVVKEDKFAWQTDEEFAREMLAGVNPLIIRRLKEFPPKSKLDPKMYGDQHSKITEEDIKSGLEGLTVAEALNQKRLYILDHHDALMPYLRKINSTKTKTYATRTLLLLKNDGTLKPLVIELSLPHPQGDQFGANSKQYFPAEEGVQKSIWQLAKAYVVVNDAGYHQLISHWLNTHAVQEPFVIATHRQLSVLHPIHKLLVPHYKDTMFINAFARQVLVNGDGLLEQTHFQSKYAMELSSYIYKEWNFTEQALPVDLIKRGVAVEDPSSPNGVKLLIEDYPFAVDGLEIWSTIKTWVTNYCSLYYKDDSAIQNDVELQSWWKEVREKGHVDKKNETWWPKLQNFNELVETCTTIIWISSALHAAVNFGQYPYGGFMPNRPTISRRLIPAVGSAEYKELESKPEKAYLKTVNSMLQTLLGVSLIEILSRHASDEVYLGQRASIEWTSDKAAVEVFENFGKKVFEVESRIIERNKDVNLKNRSGPVNVPYTLLLPSSTEGLTGRGIPNSISI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U36339
EMBL· GenBank· DDBJ
AAA79186.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp