V5Y0F7 · AF161_ALTAL
- ProteinReducing polyketide synthase AFT16-1
- GeneAFT16-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2349 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Reducing polyketide synthase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype (Probable). AF-toxin I and III are valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively, while AF II is an isoleucine derivative of 2-hydroxy-valeric acid (PubMed:15066029, PubMed:22846083, Ref.4). These derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) moiety (PubMed:15066029, PubMed:22846083, Ref.4). On cellular level, AF-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K+ after a few minutes of toxin treatment (PubMed:22846083).
The aldo-keto reductase AFTS1 catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV) by reduction of its ketone to an alcohol (PubMed:15066029).
The acyl-CoA ligase AFT1, the hydrolase AFT2 and the enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide synthase AFT9, the acyl-CoA dehydrogenase AFT10, the cytochrome P450 monooxygenase AFT11 and the oxidoreductase AFT12 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common EDA structural moiety (PubMed:12019223, PubMed:18986255, Ref.4). The exact function of each enzyme, and of additional enzymes identified within the AF-toxin clusters have still to be determined (PubMed:12019223, PubMed:18986255, Ref.4).
The aldo-keto reductase AFTS1 catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV) by reduction of its ketone to an alcohol (PubMed:15066029).
The acyl-CoA ligase AFT1, the hydrolase AFT2 and the enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide synthase AFT9, the acyl-CoA dehydrogenase AFT10, the cytochrome P450 monooxygenase AFT11 and the oxidoreductase AFT12 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common EDA structural moiety (PubMed:12019223, PubMed:18986255, Ref.4). The exact function of each enzyme, and of additional enzymes identified within the AF-toxin clusters have still to be determined (PubMed:12019223, PubMed:18986255, Ref.4).
Miscellaneous
Gene clusters encoding host-selective toxins (HSTs) are localized on conditionally dispensable chromosomes (CDCs), also called supernumerary chromosomes, where they are present in multiple copies (PubMed:12019223).
The CDCs are not essential for saprophytic growth but controls host-selective pathogenicity (PubMed:12019223).
The CDCs are not essential for saprophytic growth but controls host-selective pathogenicity (PubMed:12019223).
Pathway
Mycotoxin biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 194 | For beta-ketoacyl synthase activity | |||
Active site | 333 | For beta-ketoacyl synthase activity | |||
Active site | 382 | For beta-ketoacyl synthase activity | |||
Active site | 990 | Proton acceptor; for dehydratase activity | |||
Active site | 1170 | Proton donor; for dehydratase activity | |||
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 | secondary metabolite biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReducing polyketide synthase AFT16-1
- EC number
- Short namesPKS AFT16-1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Pleosporineae > Pleosporaceae > Alternaria > Alternaria sect. Alternaria > Alternaria alternata complex
Accessions
- Primary accessionV5Y0F7
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000444854 | 1-2349 | Reducing polyketide synthase AFT16-1 | ||
Modified residue | 2307 | O-(pantetheine 4'-phosphoryl)serine | |||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-21 | Disordered | |||
Domain | 20-462 | Ketosynthase family 3 (KS3) | |||
Region | 37-80 | Disordered | |||
Region | 578-888 | Malonyl-CoA:ACP transacylase (MAT) domain | |||
Region | 958-1092 | N-terminal hotdog fold | |||
Region | 958-1263 | Dehydratase (DH) domain | |||
Domain | 958-1269 | PKS/mFAS DH | |||
Region | 1111-1269 | C-terminal hotdog fold | |||
Region | 1976-2164 | Ketoreductase (KR) domain | |||
Domain | 2273-2347 | Carrier | |||
Domain
Multidomain protein; including 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 dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,349
- Mass (Da)257,802
- Last updated2014-02-19 v1
- MD5 ChecksumB782292165F4CC5217845DCA5D94DECA
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB872925 EMBL· GenBank· DDBJ | BAO10621.1 EMBL· GenBank· DDBJ | Genomic DNA |