P78615 · FAS2_EMEND

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 site1279For beta-ketoacyl synthase activity
Active site1519For beta-ketoacyl synthase activity
Active site1560For beta-ketoacyl synthase activity
Binding site1746Mg2+ (UniProtKB | ChEBI)
Binding site1746-1748acetyl-CoA (UniProtKB | ChEBI)
Binding site1747Mg2+ (UniProtKB | ChEBI)
Binding site1748Mg2+ (UniProtKB | ChEBI)
Binding site1772acetyl-CoA (UniProtKB | ChEBI)
Binding site1782acetyl-CoA (UniProtKB | ChEBI)
Binding site1791-1801acetyl-CoA (UniProtKB | ChEBI)
Binding site1815-1818acetyl-CoA (UniProtKB | ChEBI)
Binding site1843-1845acetyl-CoA (UniProtKB | ChEBI)
Binding site1844Mg2+ (UniProtKB | ChEBI)
Binding site1845Mg2+ (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 Processlong-chain fatty acid biosynthetic process
Biological Processsecondary metabolite 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
      fasA

Organism names

  • Taxonomic identifier
  • Strain
    • FGSC 89
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes

Accessions

  • Primary accession
    P78615

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Unable to grow on minimal medium unless supplemented with myristic acid.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004192541-1858Fatty acid synthase subunit alpha
Modified residue178O-(pantetheine 4'-phosphoryl)serine

Keywords

Interaction

Subunit

Fatty acid synthase is composed of alpha and beta subunits.

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain143-218Carrier
Compositional bias580-597Polar residues
Region580-606Disordered
Region651-848Beta-ketoacyl reductase
Domain1097-1634Ketosynthase family 3 (KS3)

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,858
  • Mass (Da)
    204,732
  • Last updated
    1997-05-01 v1
  • Checksum
    3D961E8716C9E24D
MRPEIEQELAHTLLVELLAYQFASPVRWIETQDVILAEKRTERIVEIGPADTLGGMARRTLASKYEAYDAATSVQRQILCYNKDAKEIYYDVDPVEEETESAPEAAAAPPTSAAPAAAVVAAPAPAASAPSAGPAAPVEDAPVTALDIVRTLVAQKLKKALSDVPLNKAIKDLVGGKSTLQNEILGDLGKEFGSTPEKPEDTPLDELGASMQATFNGQLGKQSSSLIARLVSSKMPGGFNITAVRKYLETRWGLGPGRQDGVLLLALTMEPASRIGSEPDAKVFLDDVANKYAANSGISLNVPTASGDGGASAGGMLMDPAAIDALTKDQRALFKQQLEIIARYLKMDLRDGQKAFVASQETQKTLQAQLDLWQAEHGDFYASGIEPSFDPLKARVYDSSWNWARQDALSMYYDIIFGRLKVVDREIVSQCIRIMNRSNPLLLEFMQYHIDNCPTERGETYQLAKELGEQLIENCKEVLGVSPVYKDVAVPTGPQTTIDARGNIEYQEVPRASARKLEHYVKQMAEGGPISEYSNRAKVQNDLRSVYKLIRRQHRLSKSSQLQFNALYKDVVRALSMNENQIMPQENGSTKKPGRNGSVRNGSPRAGKVETIPFLHLKKKNEHGWDYSKKLTGIYLDVLESAARSGLTFQGKNVLMTGAGAGSIGAEVLQGLISGGAKVIVTTSRYSREVTEYYQAMYARYGARGSQLVVVPFNQGSKQDVEALVDYIYDTKKGLGWDLDFIVPFAAIPENGREIDSIDSKSELAHRIMLTNLLRLLGSVKAQKQANGFETRPAQVILPLSPNHGTFGNDGLYSESKLALETLFNRWYSENWSNYLTICGAVIGWTRGTGLMSGNNMVAEGVEKLGVRTFSQQEMAFNLLGLMAPAIVNLCQLDPVWADLNGGLQFIPDLKDLMTRLRTEIMETSDVRRAVIKETAIENKVVNGEDSEVLYKKVIAEPRANIKFQFPNLPTWDEDIKPLNENLKGMVNLDKVVVVTGFSEVGPWGNSRTRWEMEASGKFSLEGCVEMAWIMGLIRHHNGPIKGKTYSGWVDSKTGEPVDDKDVKAKYEKYILEHSGIRLIEPELFKGYDPKKKQLLQEIVIEEDLEPFEASKETAEEFKREHGEKVEIFEVLESGEYTVRLKKGATLLIPKALQFDRLVAGQVPTGWDARRYGIPEDIIEQVDPVTLFVLVCTAEAMLSAGVTDPYEFYKYVHLSEVGNCIGSGIGGTHALRGMYKDRYLDKPLQKDILQESFINTMSAWVNMLLLSSTGPIKTPVGACATAVESVDIGYETIVEGKARVCFVGGFDDFQEEGSYEFANMKATSNAEDEFAHGRTPQEMSRPTTTTRAGFMESQGCGMQLIMSAQLALDMGVPIYGIIALTTTATDKIGRSVPAPGQGVLTTARENPGKFPSPLLDIKYRRRQLELRKRQIREWQESELLYLQEEAEAIKAQNPADFVVEEYLQERAQHINREAIRQEKDAQFSLGNNFWKQDSRIAPLRGALATWGLTVDEIGVASFHGTSTVANDKNESDVICQQMKHLGRKKGNALLGIFQKYLTGHPKGAAGAWMFNGCLQVLDSGLVPGNRNADNVDKVMEKFDYIVYPSRSIQTDGIKAFSVTSFGFGQKGAQVIGIHPKYLYATLDRAQFEAYRAKVETRQKKAYRYFHNGLVNNSIFVAKNKAPYEDELQSKVFLNPDYRVAADKKTSELKYPPKPPVATDAGSESTKAVIESLAKAHATENSKIGVDVESIDSINISNETFIERILPASEQQYCQNAPSPQSSFAGRWSAKEAVFKSLGVCSKGAGAPLKDIEIENDSNGAPTLHGVAAEAAKEAGVKHISVSISHSDMQAVAVAISQF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias580-597Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U75347
EMBL· GenBank· DDBJ
AAB41493.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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