S0DRI1 · FUB1_GIBF5

Function

function

Reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:24389666, PubMed:26662839).
L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (PubMed:26662839).
The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (PubMed:26662839).
FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (PubMed:26662839).
Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (PubMed:26662839).
Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (PubMed:26662839).

Biotechnology

Fusaric acid is phytotoxic to plants such as cotton and banana (PubMed:20955724, PubMed:23922960).
It has been shown to induce programmed cell death in plants (PubMed:16868776, PubMed:23838885).
In addition to a mild toxicity to animals, fusaric acid exhibits acanthamoebicidal, antioomycete, and antimycobacterial activities (PubMed:17927749, PubMed:21811925, PubMed:22864988).

Pathway

Mycotoxin biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site230For beta-ketoacyl synthase activity
Active site365For beta-ketoacyl synthase activity
Active site403For beta-ketoacyl synthase activity
Active site699For malonyltransferase activity
Active site1026Proton acceptor; for dehydratase activity
Active site1220Proton donor; for dehydratase activity

GO annotations

AspectTerm
Molecular Function3-oxoacyl-[acyl-carrier-protein] synthase activity
Molecular Functionfatty acid synthase activity
Molecular Functionoxidoreductase activity
Molecular Functionphosphopantetheine binding
Biological Processfatty acid biosynthetic process
Biological Processlactone biosynthetic process
Biological Processsecondary metabolite biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Reducing polyketide synthase FUB1
  • EC number
  • Alternative names
    • Fusaric acid biosynthesis protein 1

Gene names

    • Name
      FUB1
    • ORF names
      FFUJ_02105

Organism names

Accessions

  • Primary accession
    S0DRI1

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Impairs the production of fusaric acid (PubMed:24389666, PubMed:26662839).

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004373071-2410Reducing polyketide synthase FUB1
Modified residue2366O-(pantetheine 4'-phosphoryl)serine

Keywords

Expression

Induction

Expressed under high amounts of nitrogen via regulation by AREB (PubMed:24389666).
Moreover, components of the fungal-specific velvet complex VEL1 and LAE1 act also as positive regulators of expression (PubMed:24389666).
Finally, the pH regulator PACC acts as activator of FUB expression after the pH shift to alkaline ambient conditions (PubMed:24389666).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-38Polar residues
Region1-52Disordered
Domain57-479Ketosynthase family 3 (KS3)
Region608-929Malonyl-CoA:ACP transacylase (MAT) domain
Region994-1127N-terminal hotdog fold
Domain994-1307PKS/mFAS DH
Region995-1302Dehydratase (DH) domain
Region1155-1307C-terminal hotdog fold
Region1714-2026Enoyl reductase (ER) domain
Region2050-2226Ketoreductase (KR) domain
Domain2329-2406Carrier

Domain

Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,410
  • Mass (Da)
    259,533
  • Last updated
    2013-09-18 v1
  • Checksum
    FBA989E0F29DD422
MTLSNGSNGANGTSNGNGAHPSANGFHNAANGGANNGSANGGAEHDAGRPQVDGDISSAIAVIGVSGRFPGDATSPRHLWDLLKEGRNALSDVPESRFNIDGFYHPDGGRAGTLNTKQGYFLKSDVDKFDAGFFSITPEEARGMDPTQRILLELAYEGLENAGLKIDEVANQHMSCYIGACQHDYWDLQAYDMDSAPKYTATGTGPALLSNRISWFFNLKGPSVTIDTACSSTLTALHLAGQSIRNGESDSALVGGLGLHLLPNFGVFMSSMSFLSADNKCHSFDASANGYARAEGGGFVVLKRLDKALADGDTIRAVLRSTGSNQDGRTLGITQPSASRQEELIRATYASAGLSFDKTNLFEAHGTGTKVGDPIECSVIGNVFGKTREKPVYVGSVKSNIGHLEGASGLAGLVKTIYSLESGVISPTYGLEHVNPKIKLDEWKINIPTEEIKWPAGLRRASINSFGYGGANAHAVLDDAYHFLKTHNLKGHHNTKVEGVLNTGLIANGSQDVIEGTDKKSHLFLLSSHEESGIARLSQTLQAYLAETSARKLPEDQFLHRLAYTLSEKRSALPWKTYAAASTIEELQQALDGAPAKAARVPRSQALTFIFTGQGAQWFAMGRELQKYPVFQQSLHACSQYLKDFGSTWDLVEELNRDAKESIIDLPYVSQPSCTALQLSIIDLLASWGIHPQVTVGHSSGEIAAAYAKGAFDKEAAMRIAYFRGHLTGNITKTGSMAAVGLGPDRVSEYMSRVTAGKIVIACINSPASVTLSGDVEGIDEVLTFLQADDIFARKLRVTTAYHSHHMQQISEEYLNSLSGKWELKPGNPKVRMFSSVSAKAIDGTELGPAYWVANLVSPVNFSGAVTAAANAGALGKRKTSGKKGSADAMVEIGPHAALQGPLKQILDSIGDKGASPKYFSAIKRKQDAIQTTLEVVGELLVLGHQVNIPLANTYTETTSALVDLPPYAWNTANSYWHESAAVTAYKQRKHPRLELLGVRDPRSTKAEPAWHNYLRISEQPWIEHHQFQNTNIYPMAGMIVMAIEGLRQVETRADVEGYTIRDVNIGSALVVPPDQTVETRLQLTPWRSGPNVSWSHWTEFTVSSRNESGSWTTNCTGLVSTSYKHDTNSTFLDEEAAANALLNQEYKDISKSDLPSVDPTVFYTKLDESGFSLGPAFRGVKELNLFDHKAHFSMEVIDTKEFYPKKWEPAHLIHPAVLDVFVHLLISSTGDAAEIKARVPVSTASLYISADFDSTGGTKYHGFSTSKKHGATNMLSDVIAFAEGGSKALIALKGCKTVPLRGASDSSSGDGQPLGHVPVVPKKVVDVEISDAATLGQLLTGTDLASKLASYLSLLGQKRPGLRVLEYSSSTSSTLLKALTAQAEDLQGSLSSVALTTPLDGPADELTSVPETWKNKVRQEKLDLAQDPSTQGFEDVALDVIILDVEDQQGDISLVLKNAKKVLKPSGILLIANHTAAISTDLLTSTGFTSTTVSDLIIARHKPETEPPVRRVLVVTPSTTSPGLGRLITQAESDLTSRGYEVAKTDFGSIPEQATPFLTLSALDIDAPFLEGFHHETFAKLRSLFLASRGTLWLTLDTASRGLVNGLGRTIRAEHPDISFTTLGLDASAALDSASNTKTISSIIDNISRKTFGETSDSEYVIRDNQVLIERLIPNPGLKALLDSSKTGNKLSAVKIPLKQVAKPLQLSIRDHGLLDTLEYLSVPDLPEPLGDNQIEIEVGSVGLNFRDVMVAMGQMEDSTLGIECAGVVVKVGAGVQKFKVGDRVFGMHAGCFQTRVRVDPRTFQRTPDNLGDEEAASLMCTSATVVHSLIDVARLQRGESVLIHSAAGGVGQTAIRLAKHLGAEIFATVSSEKKKRLLVEEYGIKESHIFNSRDYSFADGILRLTNQRGVDVVINSLAGEALRRTWLCVAPFGRFIELGKRDIYDNSGLDMRPFLDNITFSGLDILTQVISYPDRFEAIGNQVVELLSKNAISPLNNLARYSFGEVSKAFRLMQSGGHVGKIVLYPRPDDIVPVVPDGLESFCLPHDATYVLIGGLGGIGRSVTRLLVQRGARHLVFLSRSAASRPEAQALLDEVHAQGVQAKAFAVDVAEKSQLEPVINDVKQSFPAIKGLIHCAMDLRDAVYSNMTADDWNASLRPKLLATRNLHDLLPTDLDFFICLSSIAGIIGSRGQANYNAGNTYQDALAHQRAASGLAATSINLSLVVGIGVSTERSEVFQLLKDGGLLGMDENDVLNIIKAAISGRTPTQVALGASTGGQLDKLAANDPYWFADSRFAVLNQLDRQGTGAVAGGQDWKKLIAAAASPDEVYEIVLQQLLEGVSKIIKADVEDMDSRRSLPALGIDSLVAIEIRTWLLKEFQADLSVFDIVSNDPLTGFTKKVMAKSALIA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-38Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HF679025
EMBL· GenBank· DDBJ
CCT65184.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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