S0DRI1 · FUB1_GIBF5
- ProteinReducing polyketide synthase FUB1
- GeneFUB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2410 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 230 | For beta-ketoacyl synthase activity | ||||
Sequence: C | ||||||
Active site | 365 | For beta-ketoacyl synthase activity | ||||
Sequence: H | ||||||
Active site | 403 | For beta-ketoacyl synthase activity | ||||
Sequence: H | ||||||
Active site | 699 | For malonyltransferase activity | ||||
Sequence: S | ||||||
Active site | 1026 | Proton acceptor; for dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1220 | Proton donor; for dehydratase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3-oxoacyl-[acyl-carrier-protein] synthase activity | |
Molecular Function | fatty acid synthase activity | |
Molecular Function | oxidoreductase activity | |
Molecular Function | phosphopantetheine binding | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | lactone biosynthetic process | |
Biological Process | secondary metabolite biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReducing polyketide synthase FUB1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium > Fusarium fujikuroi species complex
Accessions
- Primary accessionS0DRI1
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000437307 | 1-2410 | Reducing polyketide synthase FUB1 | |||
Sequence: MTLSNGSNGANGTSNGNGAHPSANGFHNAANGGANNGSANGGAEHDAGRPQVDGDISSAIAVIGVSGRFPGDATSPRHLWDLLKEGRNALSDVPESRFNIDGFYHPDGGRAGTLNTKQGYFLKSDVDKFDAGFFSITPEEARGMDPTQRILLELAYEGLENAGLKIDEVANQHMSCYIGACQHDYWDLQAYDMDSAPKYTATGTGPALLSNRISWFFNLKGPSVTIDTACSSTLTALHLAGQSIRNGESDSALVGGLGLHLLPNFGVFMSSMSFLSADNKCHSFDASANGYARAEGGGFVVLKRLDKALADGDTIRAVLRSTGSNQDGRTLGITQPSASRQEELIRATYASAGLSFDKTNLFEAHGTGTKVGDPIECSVIGNVFGKTREKPVYVGSVKSNIGHLEGASGLAGLVKTIYSLESGVISPTYGLEHVNPKIKLDEWKINIPTEEIKWPAGLRRASINSFGYGGANAHAVLDDAYHFLKTHNLKGHHNTKVEGVLNTGLIANGSQDVIEGTDKKSHLFLLSSHEESGIARLSQTLQAYLAETSARKLPEDQFLHRLAYTLSEKRSALPWKTYAAASTIEELQQALDGAPAKAARVPRSQALTFIFTGQGAQWFAMGRELQKYPVFQQSLHACSQYLKDFGSTWDLVEELNRDAKESIIDLPYVSQPSCTALQLSIIDLLASWGIHPQVTVGHSSGEIAAAYAKGAFDKEAAMRIAYFRGHLTGNITKTGSMAAVGLGPDRVSEYMSRVTAGKIVIACINSPASVTLSGDVEGIDEVLTFLQADDIFARKLRVTTAYHSHHMQQISEEYLNSLSGKWELKPGNPKVRMFSSVSAKAIDGTELGPAYWVANLVSPVNFSGAVTAAANAGALGKRKTSGKKGSADAMVEIGPHAALQGPLKQILDSIGDKGASPKYFSAIKRKQDAIQTTLEVVGELLVLGHQVNIPLANTYTETTSALVDLPPYAWNTANSYWHESAAVTAYKQRKHPRLELLGVRDPRSTKAEPAWHNYLRISEQPWIEHHQFQNTNIYPMAGMIVMAIEGLRQVETRADVEGYTIRDVNIGSALVVPPDQTVETRLQLTPWRSGPNVSWSHWTEFTVSSRNESGSWTTNCTGLVSTSYKHDTNSTFLDEEAAANALLNQEYKDISKSDLPSVDPTVFYTKLDESGFSLGPAFRGVKELNLFDHKAHFSMEVIDTKEFYPKKWEPAHLIHPAVLDVFVHLLISSTGDAAEIKARVPVSTASLYISADFDSTGGTKYHGFSTSKKHGATNMLSDVIAFAEGGSKALIALKGCKTVPLRGASDSSSGDGQPLGHVPVVPKKVVDVEISDAATLGQLLTGTDLASKLASYLSLLGQKRPGLRVLEYSSSTSSTLLKALTAQAEDLQGSLSSVALTTPLDGPADELTSVPETWKNKVRQEKLDLAQDPSTQGFEDVALDVIILDVEDQQGDISLVLKNAKKVLKPSGILLIANHTAAISTDLLTSTGFTSTTVSDLIIARHKPETEPPVRRVLVVTPSTTSPGLGRLITQAESDLTSRGYEVAKTDFGSIPEQATPFLTLSALDIDAPFLEGFHHETFAKLRSLFLASRGTLWLTLDTASRGLVNGLGRTIRAEHPDISFTTLGLDASAALDSASNTKTISSIIDNISRKTFGETSDSEYVIRDNQVLIERLIPNPGLKALLDSSKTGNKLSAVKIPLKQVAKPLQLSIRDHGLLDTLEYLSVPDLPEPLGDNQIEIEVGSVGLNFRDVMVAMGQMEDSTLGIECAGVVVKVGAGVQKFKVGDRVFGMHAGCFQTRVRVDPRTFQRTPDNLGDEEAASLMCTSATVVHSLIDVARLQRGESVLIHSAAGGVGQTAIRLAKHLGAEIFATVSSEKKKRLLVEEYGIKESHIFNSRDYSFADGILRLTNQRGVDVVINSLAGEALRRTWLCVAPFGRFIELGKRDIYDNSGLDMRPFLDNITFSGLDILTQVISYPDRFEAIGNQVVELLSKNAISPLNNLARYSFGEVSKAFRLMQSGGHVGKIVLYPRPDDIVPVVPDGLESFCLPHDATYVLIGGLGGIGRSVTRLLVQRGARHLVFLSRSAASRPEAQALLDEVHAQGVQAKAFAVDVAEKSQLEPVINDVKQSFPAIKGLIHCAMDLRDAVYSNMTADDWNASLRPKLLATRNLHDLLPTDLDFFICLSSIAGIIGSRGQANYNAGNTYQDALAHQRAASGLAATSINLSLVVGIGVSTERSEVFQLLKDGGLLGMDENDVLNIIKAAISGRTPTQVALGASTGGQLDKLAANDPYWFADSRFAVLNQLDRQGTGAVAGGQDWKKLIAAAASPDEVYEIVLQQLLEGVSKIIKADVEDMDSRRSLPALGIDSLVAIEIRTWLLKEFQADLSVFDIVSNDPLTGFTKKVMAKSALIA | ||||||
Modified residue | 2366 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-38 | Polar residues | ||||
Sequence: MTLSNGSNGANGTSNGNGAHPSANGFHNAANGGANNGS | ||||||
Region | 1-52 | Disordered | ||||
Sequence: MTLSNGSNGANGTSNGNGAHPSANGFHNAANGGANNGSANGGAEHDAGRPQV | ||||||
Domain | 57-479 | Ketosynthase family 3 (KS3) | ||||
Sequence: SSAIAVIGVSGRFPGDATSPRHLWDLLKEGRNALSDVPESRFNIDGFYHPDGGRAGTLNTKQGYFLKSDVDKFDAGFFSITPEEARGMDPTQRILLELAYEGLENAGLKIDEVANQHMSCYIGACQHDYWDLQAYDMDSAPKYTATGTGPALLSNRISWFFNLKGPSVTIDTACSSTLTALHLAGQSIRNGESDSALVGGLGLHLLPNFGVFMSSMSFLSADNKCHSFDASANGYARAEGGGFVVLKRLDKALADGDTIRAVLRSTGSNQDGRTLGITQPSASRQEELIRATYASAGLSFDKTNLFEAHGTGTKVGDPIECSVIGNVFGKTREKPVYVGSVKSNIGHLEGASGLAGLVKTIYSLESGVISPTYGLEHVNPKIKLDEWKINIPTEEIKWPAGLRRASINSFGYGGANAHAVLDD | ||||||
Region | 608-929 | Malonyl-CoA:ACP transacylase (MAT) domain | ||||
Sequence: TFIFTGQGAQWFAMGRELQKYPVFQQSLHACSQYLKDFGSTWDLVEELNRDAKESIIDLPYVSQPSCTALQLSIIDLLASWGIHPQVTVGHSSGEIAAAYAKGAFDKEAAMRIAYFRGHLTGNITKTGSMAAVGLGPDRVSEYMSRVTAGKIVIACINSPASVTLSGDVEGIDEVLTFLQADDIFARKLRVTTAYHSHHMQQISEEYLNSLSGKWELKPGNPKVRMFSSVSAKAIDGTELGPAYWVANLVSPVNFSGAVTAAANAGALGKRKTSGKKGSADAMVEIGPHAALQGPLKQILDSIGDKGASPKYFSAIKRKQDA | ||||||
Region | 994-1127 | N-terminal hotdog fold | ||||
Sequence: LELLGVRDPRSTKAEPAWHNYLRISEQPWIEHHQFQNTNIYPMAGMIVMAIEGLRQVETRADVEGYTIRDVNIGSALVVPPDQTVETRLQLTPWRSGPNVSWSHWTEFTVSSRNESGSWTTNCTGLVSTSYKHD | ||||||
Domain | 994-1307 | PKS/mFAS DH | ||||
Sequence: LELLGVRDPRSTKAEPAWHNYLRISEQPWIEHHQFQNTNIYPMAGMIVMAIEGLRQVETRADVEGYTIRDVNIGSALVVPPDQTVETRLQLTPWRSGPNVSWSHWTEFTVSSRNESGSWTTNCTGLVSTSYKHDTNSTFLDEEAAANALLNQEYKDISKSDLPSVDPTVFYTKLDESGFSLGPAFRGVKELNLFDHKAHFSMEVIDTKEFYPKKWEPAHLIHPAVLDVFVHLLISSTGDAAEIKARVPVSTASLYISADFDSTGGTKYHGFSTSKKHGATNMLSDVIAFAEGGSKALIALKGCKTVPLRGASDS | ||||||
Region | 995-1302 | Dehydratase (DH) domain | ||||
Sequence: ELLGVRDPRSTKAEPAWHNYLRISEQPWIEHHQFQNTNIYPMAGMIVMAIEGLRQVETRADVEGYTIRDVNIGSALVVPPDQTVETRLQLTPWRSGPNVSWSHWTEFTVSSRNESGSWTTNCTGLVSTSYKHDTNSTFLDEEAAANALLNQEYKDISKSDLPSVDPTVFYTKLDESGFSLGPAFRGVKELNLFDHKAHFSMEVIDTKEFYPKKWEPAHLIHPAVLDVFVHLLISSTGDAAEIKARVPVSTASLYISADFDSTGGTKYHGFSTSKKHGATNMLSDVIAFAEGGSKALIALKGCKTVPLR | ||||||
Region | 1155-1307 | C-terminal hotdog fold | ||||
Sequence: LPSVDPTVFYTKLDESGFSLGPAFRGVKELNLFDHKAHFSMEVIDTKEFYPKKWEPAHLIHPAVLDVFVHLLISSTGDAAEIKARVPVSTASLYISADFDSTGGTKYHGFSTSKKHGATNMLSDVIAFAEGGSKALIALKGCKTVPLRGASDS | ||||||
Region | 1714-2026 | Enoyl reductase (ER) domain | ||||
Sequence: GLLDTLEYLSVPDLPEPLGDNQIEIEVGSVGLNFRDVMVAMGQMEDSTLGIECAGVVVKVGAGVQKFKVGDRVFGMHAGCFQTRVRVDPRTFQRTPDNLGDEEAASLMCTSATVVHSLIDVARLQRGESVLIHSAAGGVGQTAIRLAKHLGAEIFATVSSEKKKRLLVEEYGIKESHIFNSRDYSFADGILRLTNQRGVDVVINSLAGEALRRTWLCVAPFGRFIELGKRDIYDNSGLDMRPFLDNITFSGLDILTQVISYPDRFEAIGNQVVELLSKNAISPLNNLARYSFGEVSKAFRLMQSGGHVGKIVL | ||||||
Region | 2050-2226 | Ketoreductase (KR) domain | ||||
Sequence: ATYVLIGGLGGIGRSVTRLLVQRGARHLVFLSRSAASRPEAQALLDEVHAQGVQAKAFAVDVAEKSQLEPVINDVKQSFPAIKGLIHCAMDLRDAVYSNMTADDWNASLRPKLLATRNLHDLLPTDLDFFICLSSIAGIIGSRGQANYNAGNTYQDALAHQRAASGLAATSINLSLV | ||||||
Domain | 2329-2406 | Carrier | ||||
Sequence: EVYEIVLQQLLEGVSKIIKADVEDMDSRRSLPALGIDSLVAIEIRTWLLKEFQADLSVFDIVSNDPLTGFTKKVMAKS |
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 statusComplete
- Length2,410
- Mass (Da)259,533
- Last updated2013-09-18 v1
- ChecksumFBA989E0F29DD422
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-38 | Polar residues | ||||
Sequence: MTLSNGSNGANGTSNGNGAHPSANGFHNAANGGANNGS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HF679025 EMBL· GenBank· DDBJ | CCT65184.1 EMBL· GenBank· DDBJ | Genomic DNA |