A0A1E4SU68 · A0A1E4SU68_9ASCO

Function

function

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.

Catalytic activity

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site277For acetyltransferase activity
Active site1818For malonyltransferase activity

GO annotations

AspectTerm
Cellular Componentfatty acid synthase complex
Molecular Function(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity
Molecular Function[acyl-carrier-protein] S-acetyltransferase activity
Molecular Function[acyl-carrier-protein] S-malonyltransferase activity
Molecular Functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
Molecular Functionfatty acid synthase activity
Molecular Functionfatty acyl-[ACP] hydrolase activity
Molecular Functionfatty-acyl-CoA synthase activity
Biological Processfatty acid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fatty acid synthase subunit beta
  • EC number

Including 5 domains:

  • Recommended name
    3-hydroxyacyl-[acyl-carrier-protein] dehydratase
  • EC number
  • Recommended name
    Enoyl-[acyl-carrier-protein] reductase [NADH]
  • EC number
  • Recommended name
    [Acyl-carrier-protein] acetyltransferase
  • EC number
  • Recommended name
    [Acyl-carrier-protein] malonyltransferase
  • EC number
  • Recommended name
    S-acyl fatty acid synthase thioesterase
  • EC number

Gene names

    • ORF names
      CANARDRAFT_30438

Organism names

  • Taxonomic identifier
  • Strain
    • NRRL YB-2248
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Pichiaceae > Ogataea > Ogataea/Candida clade

Accessions

  • Primary accession
    A0A1E4SU68

Proteomes

Subcellular Location

Interaction

Subunit

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

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1674-2028Malonyl-CoA:ACP transacylase (MAT)

Sequence similarities

Belongs to the fungal fatty acid synthetase subunit beta family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,061
  • Mass (Da)
    228,039
  • Last updated
    2017-01-18 v1
  • Checksum
    9E299D39503F12CC
MATNRPLVVAHGSIETTILTPPSNYLFYQQLTTDFYKSLPNVTEGFADDDEPSSKAELLMMFLGYIISSNSIESEKVDAVKLILDEFDTRFLQDRDLHSFAAELLTSESHPTTLPKIKNHLIKNYYSGKVFLDKSYGLKINGATHSVLFNAAMKKEALVFSVFGGQGNTDDYFEELREVYTVYNGLVSDFLIKVQSKLQSLISSTSDIDRVYTHGFDLINWLENPEQTPTTEHLLSAPVSCPLICVTQLCHFIITCKILGVNPAQVIEALEGSTGHSQGIVTAVALASVDSWETLEINALKAIEFLFYLSVRCLQAYPSTSLSPFAVKDSQESGEGQPGPMLSIRDLSIEQVTKFIDQTNQHLPEAKHISISLVNGARNLVVTGPPESLYGLNLNLRNAKAPSGLEQSRIPHSERKLKFSSRFLPIMSPFHSKLLAPANERIAADLKKAGLSFNQADLKIPVFDTYDGSNLMHYKGDLSTRITELITLYTVNWEVATNFKATHIIDFGPGGVSGLGVLTHRNKEGTGASVIVAGALEASNEDSEFGYKQELFDTSKSSLKFAPNWLKEYQPKLAKTKDGKVYVDTKFSRLLGRAPLMVPGMTPTTVSPDFVAATIRAGYHIELAGGGYFNATQMQAALKKVTENVTPGSGIGLNLIYVSPRMLQWGIPMIRELREKGFPIQSMSIGAGVPSLEVATEYIETLGLTHLGLKPGSIDAINQCITIAKTHPTFPIVLQWTGGRGGGHHSYEDFHQPILQMYSKIRRCPNIILIAGSGFGSAEDTYPYLTGKWSTQFEYPEMPFDGVLFGSRVMTALEAKTSPDAKKAIASCSGVADSEWEKTYKKPTGGILTVRSEMGEPIHKIATRAVVFWKEMDDTIFSLPKNKMIDALAKKKDYIISKLNSDFQKTWFGKNDEGVCDIQEMTYSQVAQRCVELMYVRKSSRWIDVSLRNFTAQFLRRIEERFSTKSTTSVIQRFSQLDSPDEALEAVFKAYPESKVQLINGEDYDYFIAQCTSPGQKPVPFVPVLDERFEVFFKKDSLWQSEDLEAVVDEDVQRTCILHGPVAAQFTNKVDEPIKEILDSIHEGHISKLLEEVYGGDASKIPVVEYFSDKSTEKVSSVPGVTITESANEVVYSIGSTLPESDAWFKLLAGSELSWRHAFISSAIVVQDSNHVVNPAKKVLAPAKNLVVKISYPEDPSKTVISVSEPLKGKSREIVNVSTTDPKSIKLQLIEHRTADGSAIPLELLYTYKPSDGFAPILEVMEGRNERIKAFYWKVWFGLSSPVDLDFDVTSRIDGGSMEITPKAIAELTHAIGNSCEYFVPRAGRDQLAPMDFAIVIGWRAIMKAIFPSTVDGDILRLVHLSNAYRMFPGAEPLKAGDKVSSDAEIISVVNGETGKTVEVVGTIYRDGAAIMEVTSAFFYRGTYNDFDKTFQKTSETPAEVKLTTAKDVAVLKSKEWFHITDSVDLLNKTLTFRCKSVYKFNSSSVYSSVITTGAAYYELSSKEVKQVAEINYEAAYSHGNPVIDYLNRNGSPIEQPLMFENAIPLSGTLSTKAPGSNEIYAAVSGDFNPIHVSRVFSSYANLPGTITHGMFSSASVRSLVEMYAANGVAPRVRAYKATFVGMVLPNDELSTKLEHVGMINGRKIVKIETKKVETDEVVLAGEAEIDQPVSTFVFTGQGSQEQGMGMDLYNSSEVAKAVWDRADVHFVENYGFSILEIVKNNPNELTVHFGGPKGRKIRESYKTMMFETVDADGKLKSEKIFKEIDDTTSTYTFKSPTGLLSATQFTQPALTLMEKAAFEDMKAKGLVPAESMFAGHSLGEYSALSSLADVMPIESLVDVVFYRGMTMQVAVPRDALGRSNYGMCAVNPSRISPTFTDAALRFVIDHISKQTGWLLEIVNYNVENQQYVTAGDLRGLDTLTNTLNVFKLQKIDIVKLQEMLSLEKVAEHLTEIVAEVSKKSLAKPQPIDLERGFACIPLKGISVPFHSSYLRSGVKPFQRFLVKKIPKSAVKPASLIGKYIPNLTAKPFQLTKEYFEDVYQLTGSEKIKAVLDNWEHYESS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV453870
EMBL· GenBank· DDBJ
ODV82972.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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