A0A1W2FW33 · A0A1W2FW33_KIBAR

Function

function

Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain.

Catalytic activity

  • (2E)-decenoyl-[ACP] + NADPH + H+ = decanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • (2E)-dodecenoyl-[ACP] + NADPH + H+ = dodecanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • (2E)-hexadecenoyl-[ACP] + NADPH + H+ = hexadecanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • (2E)-hexenoyl-[ACP] + NADPH + H+ = hexanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • (2E)-octadecenoyl-[ACP] + NADPH + H+ = octadecanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • (2E)-octenoyl-[ACP] + NADPH + H+ = octanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • (2E)-tetradecenoyl-[ACP] + NADPH + H+ = tetradecanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • (3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O
    This reaction proceeds in the forward direction.
  • (3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O
    This reaction proceeds in the forward direction.
  • (3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O
    This reaction proceeds in the forward direction.
  • (3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] + H2O
    This reaction proceeds in the forward direction.
  • (3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O
    This reaction proceeds in the forward direction.
  • (3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] + H2O
    This reaction proceeds in the forward direction.
  • (3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O
    This reaction proceeds in the forward direction.
  • (3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] + H2O
    This reaction proceeds in the forward direction.
  • 3-oxobutanoyl-[ACP] + NADPH + H+ = (3R)-hydroxybutanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • 3-oxodecanoyl-[ACP] + NADPH + H+ = (3R)-hydroxydecanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • 3-oxododecanoyl-[ACP] + NADPH + H+ = (3R)-hydroxydodecanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • 3-oxohexadecanoyl-[ACP] + NADPH + H+ = (3R)-hydroxyhexadecanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • 3-oxohexanoyl-[ACP] + NADPH + H+ = (3R)-hydroxyhexanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • 3-oxooctadecanoyl-[ACP] + NADPH + H+ = (3R)-hydroxyoctadecanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • 3-oxooctanoyl-[ACP] + NADPH + H+ = (3R)-hydroxyoctanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • 3-oxotetradecanoyl-[ACP] + NADPH + H+ = (3R)-hydroxytetradecanoyl-[ACP] + NADP+
    This reaction proceeds in the forward direction.
  • hexadecanoyl-[ACP] + malonyl-[ACP] + H+ = 3-oxooctadecanoyl-[ACP] + holo-[ACP] + CO2
    This reaction proceeds in the forward direction.
  • hexanoyl-[ACP] + malonyl-[ACP] + H+ = 3-oxooctanoyl-[ACP] + holo-[ACP] + CO2
    This reaction proceeds in the forward direction.
  • octanoyl-[ACP] + malonyl-[ACP] + H+ = 3-oxodecanoyl-[ACP] + holo-[ACP] + CO2
    This reaction proceeds in the forward direction.
  • tetradecanoyl-[ACP] + malonyl-[ACP] + H+ = 3-oxohexadecanoyl-[ACP] + holo-[ACP] + CO2
    This reaction proceeds in the forward direction.
  • hexadecanoyl-[ACP] + H2O = hexadecanoate + holo-[ACP] + H+
    This reaction proceeds in the forward direction.
    EC:3.1.2.14 (UniProtKB | ENZYME | Rhea)
  • tetradecanoyl-[ACP] + H2O = tetradecanoate + holo-[ACP] + H+
    This reaction proceeds in the forward direction.
    EC:3.1.2.14 (UniProtKB | ENZYME | Rhea)
  • a (3R)-hydroxyacyl-[ACP] + NADP+ = a 3-oxoacyl-[ACP] + NADPH + H+
    This reaction proceeds in the backward direction.
    EC:1.1.1.100 (UniProtKB | ENZYME | Rhea)
  • a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
    This reaction proceeds in the forward direction.
    EC:4.2.1.59 (UniProtKB | ENZYME | Rhea)
  • a 2,3-saturated acyl-[ACP] + NADP+ = a (2E)-enoyl-[ACP] + NADPH + H+
    This reaction proceeds in the backward direction.
    EC:1.3.1.39 (UniProtKB | ENZYME | Rhea)
  • a fatty acyl-[ACP] + malonyl-[ACP] + H+ = a 3-oxoacyl-[ACP] + holo-[ACP] + CO2
    This reaction proceeds in the forward direction.
    EC:2.3.1.41 (UniProtKB | ENZYME | Rhea)
  • holo-[ACP] + acetyl-CoA = acetyl-[ACP] + CoA
    This reaction proceeds in the forward direction.
    EC:2.3.1.38 (UniProtKB | ENZYME | Rhea)
  • acetyl-[ACP] + malonyl-[ACP] + H+ = 3-oxobutanoyl-[ACP] + holo-[ACP] + CO2
    This reaction proceeds in the forward direction.
  • butanoyl-[ACP] + malonyl-[ACP] + H+ = 3-oxohexanoyl-[ACP] + holo-[ACP] + CO2
    This reaction proceeds in the forward direction.
  • decanoyl-[ACP] + malonyl-[ACP] + H+ = 3-oxododecanoyl-[ACP] + holo-[ACP] + CO2
    This reaction proceeds in the forward direction.
  • dodecanoyl-[ACP] + malonyl-[ACP] + H+ = 3-oxotetradecanoyl-[ACP] + holo-[ACP] + CO2
    This reaction proceeds in the forward direction.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site943Proton acceptor; for dehydratase activity
Active site1107Proton donor; for dehydratase activity

GO annotations

AspectTerm
Molecular Function(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity
Molecular Function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
Molecular Function3-oxoacyl-[acyl-carrier-protein] synthase activity
Molecular Function[acyl-carrier-protein] S-acetyltransferase activity
Molecular Functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
Molecular Functionfatty acid synthase activity
Molecular Functionfatty acyl-[ACP] hydrolase activity
Molecular Functionphosphopantetheine binding
Biological Processantibiotic biosynthetic process
Biological Processfatty acid biosynthetic process
Biological Processpolyketide biosynthetic process
Biological Processtoxin biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • Acyl transferase domain-containing protein

Gene names

    • ORF names
      SAMN05661093_09424

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 43828
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Kibdelosporangium

Accessions

  • Primary accession
    A0A1W2FW33

Proteomes

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain16-442Ketosynthase family 3 (KS3)
Region910-1032N-terminal hotdog fold
Domain910-1198PKS/mFAS DH
Region1046-1198C-terminal hotdog fold
Domain2455-2532Carrier

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,813
  • Mass (Da)
    305,993
  • Last updated
    2017-06-07 v1
  • Checksum
    D38950F8D5B0E3FB
MNSVHSSSSEAESSAHEGIAVVGIGCRFPGHVSSADDLWRLLLDERDAVQAVPKDRWTGAAFYDHDASRPGHLRTQAGGYVDDVAAFDAHFFGIAPTEAARMDPQQRLFLETTWEALQDAGIVPELLAGTKTAVYAGVSGHDYGIIQLNPENRYLLGGHTMAGVTNCIVANRVSYLLDLRGPSMIVDTACSSSLVAIHLACRSIRSGEATMAIAGGVGALLIPETTIAFSQGTFLSPEGRSKSFSKSADGYVRSEGSGTVVLKPLSAAVADGDRIYAVIRGTATNSDGRTNGISVPSEEAQAQMILDACRDAGVAPTSIGYIEAHGTGTSVGDPIEARALGKALGSGRNGQGPCIVGAVKSNMGHLEPAAGIAGMIKACLVVSKGEIPANIHAEEPNPAIPFEELGLRLATARQPWPGDGPRLAGVNSFGFGGSNAHVILEGVAETDRDEETQAATHEQVLFTLSAKTKDALSAYVDSYADFLDEPRGAAALPAIASTQAQARPHYDHRLAIVGSSVDELRATLRDIQAGSSPDSVYSGVKASTAASVAFVFSGQGPQWWGMARELLDESEVFRQTVERVDAELGKYADWSVMEELRRDEASSRIGETFIAQPAVFAVQVGLASLWQSWGIAPSAVVGHSIGEVAAACVSGALSFEDAVRVIFHRSRVQQKASGKGKMLAVGLPPSEVESRIAAYRGRVEVAAHNGPESVALAGDPDALEEIERELGRDKIFCRMLQVSVAFHSHHMDPLKDELLASLAGITSGPSSIPMYSTVTADVVPTGALDAGYWWQNIRQPVMFAPTVDRLIEDQHLAFVELGPHPIHATAISELLEKRRAEGVVVASLHRKQSDRHTLLNSLASLYVAGYDPNWAGVFDGITGRVQVPFYPWQRETYWLETPTSRGRRFPSLNHPLVGTENRAADEPGKRVWELVLDPIRFPWLDDHRVQGPIVFPAAAYLDMVFGCAQDAFGDGPFSLEDVEFRRALFVFDDRPAPVVQVVLTQAMHFSVYSRQDSDAEWTLHSVGTLRRGAPTTALPKPISELQAECPVEIDPAELYAVLGRNGLALGPTFRAAVQFWRSDRKCLAQLETPAASADEAPRHAIHPGVLDSCITTLPVAYGDVLTGDVVNHQAKMLYLPVEVKRLSFHTRPSGRLFVYAQAHATDDPMFSSGDFWIVDEDGTIVAEFDGLKFKSITRSADDGDALANWFYDFRWHPAAVHRKTRMPADFLASDTTVQAAVEPLLDELRNWPVNRGYHAVTEAKMNRLCIDYVTEALHNLDMDLTEGRRFTLDEAAAEMGVHDKHRRYLGRLLELLAQHGIVENDTATWHVLRTPERVDTGSDLARLRREHPECESEYALLERCGKELATVLRDEVNPVELIFPEHEFQSVVDLYTTSFSFEKTNRIISEVVAQCMRSLPADRPVRVLEIGAGTGGTTGFVLSELPRDRAEYVYSDVGQLFLAKARERFAEYDFVDYRILDIEQDVEEQGFDPHYYDIVVASNVLHATPSLRATLANVQRLMTSQGMLLIMEATVPPHWVDLTFGMTEGWWKFDDHDVRPSYPVLTEAQWLDFLPTTGFEHVQVLSDKNTPEESGNSVIVARGQVVDLEPHQPRAQQGPWVVLADAEGVGERYLDLVGDAAAGSVLVTRGEAFEQVDARSFRVRPTSSEDLKRVLEQVRDHAGEVAGVLHLWNLDFAGSELSTELLPEIESQGAYSVVALVRAVEQVNWAKQPRFWVATSGAQVLDQAERVAPAQLPSWGIVRVLLNEQISLPAKIIDFDPATSNAGQRASQLLDELLHVRTADEEVAFRGDERFVDRLEHISPAEFEASVATPTRVSDETPFSLAVPSEHAIDQLRYEAKPLSELGRGEVAIRPLATGLNFRDVMLTLGMLAEGATFGGFYDDNLGVECAGVVTQVGADVEGLAPGDRVIAFARECFSNLVATDARLVFKSPSNLSDVEAATLPMAYLTAWYALVEVGRLRAGARVLIHAAAGGVGLAAVHIAQALGATVLATAGSEEKRGHLRSLGVEQVYDSRSLAFAEEIRQRYDGVDIVLNSLQGETIPKSLELLRPRGRFVEIGKKDIYENYQLGLKPFGNNLSYAAVDIDRLLLEDPALCRQVMTEVLDGVAAGTLPALPHTDFGAGDVAAAFRYMANAKQIGKVVVELAPDTELLVHRTSSGQETLDAEGTYLVTGGYTGFGLRTAQWLVEQSARTVVLVGRRAKTDAENEATIESMRAQGATVVLERADVSIEDEVKGLIERIAPLPPLKGIFHAAMVLDDVSLADMTEEQFLSAVRPKVDGAWHLHNHTRELDLDAFVMYSSMSWYIGTPGQANYSAANGFLEALAAYRRDMGLPALTVNWGAIGEVGFIARNKVDTLARMGWTAISPDQALAFVGRCLAQGVSRASVFGVNFAKMSQVMPSFRSSSRLAHLSMEGASGSGAGGTEGLRAELLELEEDAREPRLVAALSEQIARIFDMPVERLAHDVALTDLGMDSLMAGQIRNALAKHLEIDFPTMGLMRGPTVVELTKEVLGQVFDGAAGAQPESAMQAAGPERWIHTVQGRSNLASLRVFTLPFVGGAASVFAPWPDYLPDSVEVVALQAPGREDRINEVPIESMPEFIAELADAMLPYLDRSFAIYGHSMGGLLAYELTKYLEQQFAEVPTKLIIAGWPSAIHVEDYVRGLKHLRDGQIVGGESDDRVLEVLRDNGLLMGPIADENSIKPLMPAVRADLRMLGDYRFSDGVLLRAPITVLHGEEDPLFAEDQLRAWEKLTSGGFSMTTVPGGHLFIQNPSAEVMDTIARELSVKDTYPMFTNL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FWXV01000012
EMBL· GenBank· DDBJ
SMD25846.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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