O65040 · O65040_DOLUC

Function

function

Introduction of a cis double bond between carbons of the acyl chain.

Cofactor

Protein has several cofactor binding sites:
Fe cation (UniProtKB | Rhea| CHEBI:24875 )

Note: Binds 2 iron ions per subunit.
Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 2 Fe2+ ions per subunit.

Features

Showing features for binding site.

139650100150200250300350
TypeIDPosition(s)Description
Binding site138Fe cation 1 (UniProtKB | ChEBI)
Binding site176Fe cation 1 (UniProtKB | ChEBI)
Binding site176Fe cation 2 (UniProtKB | ChEBI)
Binding site179Fe cation 1 (UniProtKB | ChEBI)
Binding site229Fe cation 2 (UniProtKB | ChEBI)
Binding site262Fe cation 2 (UniProtKB | ChEBI)
Binding site262Fe cation 1 (UniProtKB | ChEBI)
Binding site265Fe cation 2 (UniProtKB | ChEBI)

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 Componentchloroplast stroma
Molecular Functionacyl-[acyl-carrier-protein] desaturase activity
Molecular Functionmetal ion binding
Biological Processfatty acid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acyl-[acyl-carrier-protein] desaturase
  • EC number

Gene names

    • Name
      fad1

Organism names

Accessions

  • Primary accession
    O65040

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the fatty acid desaturase type 2 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    396
  • Mass (Da)
    45,231
  • Last updated
    1998-08-01 v1
  • Checksum
    0101A758556D5C57
MALKLNAINFQSPKCSSFGLPPVVSLRSPKLSVAATLRSGLRDVETVKKTFSPAREVHVQVTHSMAPQKIEIFKAMEDWAENNILVHLKNVEKCPQPQDFLPDPASDEFHDQIKELRERAKEIPDDYFVVLVGDMITEEALPTYQTMLNTWDGVRDETGASPTSWAIWTRAWTAEENRHGDPLNKYLYLSGRVDMKQIEKTIQYLIGSGMDPRTENSPYLGFIYTSFQERATFISHGNTARLARDHGDFKLAQICGTIASDEKRHETAYTKIVEKLFEIDPDGTVLAFGDMMKKKISMPDHFMYDGRDDNLFDHFSSVAQRLGVYTAKDYADILEHLVGRWKVEKLTGLSAEGQKAQDYVCGLPPRIRRLEERAQIRAKQAPRLPFSWIYDREVQL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF051134
EMBL· GenBank· DDBJ
AAC05293.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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