P43098 · FAS2_CANAX

  • Protein
    Fatty acid synthase subunit alpha
  • Gene
    FAS2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.

Catalytic activity

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site1304For beta-ketoacyl synthase activity
Active site1546For beta-ketoacyl synthase activity
Active site1587For beta-ketoacyl synthase activity
Binding site1771Mg2+ (UniProtKB | ChEBI)
Binding site1771-1773acetyl-CoA (UniProtKB | ChEBI)
Binding site1772Mg2+ (UniProtKB | ChEBI)
Binding site1773Mg2+ (UniProtKB | ChEBI)
Binding site1797acetyl-CoA (UniProtKB | ChEBI)
Binding site1807acetyl-CoA (UniProtKB | ChEBI)
Binding site1816-1826acetyl-CoA (UniProtKB | ChEBI)
Binding site1840-1843acetyl-CoA (UniProtKB | ChEBI)
Binding site1870-1872acetyl-CoA (UniProtKB | ChEBI)
Binding site1871Mg2+ (UniProtKB | ChEBI)
Binding site1872Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentfatty acid synthase complex
Molecular Function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
Molecular Function3-oxoacyl-[acyl-carrier-protein] synthase activity
Molecular Functionfatty acid synthase activity
Molecular Functionfatty-acyl-CoA synthase activity
Molecular Functionholo-[acyl-carrier-protein] synthase activity
Molecular Functionmagnesium ion binding
Biological Processmitotic nuclear membrane biogenesis
Biological Processpalmitic acid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fatty acid synthase subunit alpha
  • EC number

Including 3 domains:

  • Recommended name
    Acyl carrier
  • Recommended name
    3-oxoacyl-[acyl-carrier-protein] reductase
  • EC number
  • Alternative names
    • Beta-ketoacyl reductase
  • Recommended name
    3-oxoacyl-[acyl-carrier-protein] synthase
  • EC number
  • Alternative names
    • Beta-ketoacyl synthase

Gene names

    • Name
      FAS2

Organism names

  • Taxonomic identifier
  • Strain
    • 4918
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida

Accessions

  • Primary accession
    P43098

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Miscellaneous

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001802841-1885Fatty acid synthase subunit alpha
Modified residue181O-(pantetheine 4'-phosphoryl)serine

Keywords

Interaction

Subunit

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region92-140Disordered
Domain146-221Carrier
Domain1121-1661Ketosynthase family 3 (KS3)

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,885
  • Mass (Da)
    207,589
  • Last updated
    1995-11-01 v1
  • Checksum
    4835D57F362372E0
MKPEIEQELSHTLLTELLAYQFASPVRWIETQDVFLKQHNTERIIEIGPSPTLAGMANRTIKAKYESYDAALSLQRQVLCYSKDAKEIYYKPDPADLAPKETPKQEESTPSAPAAATPTPAAAAAPTPAPAPASAGPVESIPDEPVKANLLIHVLVAQKLKKPLDAVPMTKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEDTPLEELAEQFQDSFSGQLGKTSTSLIGRLMSSKMPGGFSITTARKYLESRFGLGAGRQDSVLLMALTNEPANRLGSEADAKTFFDGIAQKYASSAGISLSSGAGSGAGAANSGGAVVDSAALDALTAENKKLAKQQLEVLARYLQSRLKQGSLKSFIKEKEASAVLQKELDLWEAEHGEFYAKGIQPTFSALKSRTYDSYWNWARQDVLSMYFDIIFGKLTSVDRETINQCIQIMNRANPTLIKFMQYHIDHCPEYKGETYKLAKRLGQQLIDNCKQVLTEDPVYKDVSRITGPKTKVSAKGNIEYEETQKDSVRKFEQYVYEMAQGGAMTKVSQPTIQEDLARVYKAISKQASKDSKLELQRVYEDLLKVVESSKEIETEQLTKDILQAATVPTTPTEEVDDPCTPSSDDEIASLPDKTSIIQPVSSTIPSQTIPFLHIQKKTKDGWEYNKKLSSLYLDGLESAAINGLTFKDKYVLVTGAGAGSIGAEILQGLISGGAKVIVTTSRFSKKVTEYYQNMYARYGAAGSTLIVVPFNQGSKQDVDALVQYIYDEPKKGGLGWDLDAIIPFAAIPENGNGLDNIDSKSEFAHRIMLTNLLRLLGAVKSKKPTDTRPAQCILPLSPNHGTFGFDGLYSESKISLETLFNRWYSEDWGSKLTVCGAVIGWTRGTGLMSANNIIAEGIEKLGVRTFSQKEMAFNILGLLTPEIVQLCQEEPVMADLNGGLQFIDNLKDFTSKLRTDLLETADIRRAVSIESAIEQKVVNGDNVDANYSKVMVEPRANMKFDFPTLKSYDEIKQIAPELEGMLDLENVVVVTGFAEVGPWGNSRTRWEMEAYGEFSLEGAIEMAWIMGFIKYHNGNLQGKPYSGWVDAKTQTPIDEKDIKSKYEEEILEHSGIRLIEPELFNGYDPKKKQMIQEIVVQHDLEPFECSKETAEQYKHEHGEKCEIFEIEESGEYTVRILKGATLYVPKALRFDRLVAGQIPTGWDARTYGIPEDTISQVDPITLYVLVATVEALLSAGITDPYEFYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYADKPVQNDILQESFINTMSAWVNMLLLSSSGPIKTPVGACATAVESVDIGIETILSGKAKVVLVGGYDDFQEEGSYEFANMNATSNSIEEFKHGRTPKEMSRPTTTTRNGFMEAQGSGIQVIMTADLALKMGVPIHAVLAMTATATDKIGRSVPAPGKGILTTAREHHGNLKYPSPLLNIKYRKRQLNKRLEQIKSWEETELSYLQEEAELAKEEFGDEFSMHEFLKERTEEVYRESKRQVSDAKKQWGNSFYKSDPRIAPLRGALAAFNLTIDDIGVASFHGTSTVANDKNESATINNMMKHLGRSEGNPVFGVFQKYLTGHPKGAAGAWMLNGAIQILESGLVPGNRNADNVDKLLEQYEYVLYPSRSIQTDGIKAVSVTSFGFGQKGAQAVVVHPDYLFAVLDRSTYEEYATKVSARNKKTYRYMHNAITRNTMFVAKDKAPYSDELEQPVYLDPLARVEENKKKLVFSDKTIQSNQSYVGEVAQKTAKALSTLNKSSKGVGVDVELLSAINIDNETFIERNFTGNEVEYCLNTAHPQASFTGTWSAKEAVFKALGVESKGAGASLIDIEITRDVNGAPKVILHGEAKKAAAKAGVKNVNISISHDDFQATAVALSEF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L29063
EMBL· GenBank· DDBJ
AAA34345.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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