G1XTZ5 · AR274_ARTOA
- ProteinShort chain dehydrogenase AOL_s00215g274
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids322 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sesquiterpenyl epoxy-cyclohexenoids (SECs) such as anthrobotrisins and arthrosporols, metabolites that possess a novel hybrid carbon skeleton consisting of a polyketide-derived epoxycyclohexenol combined with a terpenoid-derived monocyclic sesquiterpenol substructure (PKS-PTS hybrid) (PubMed:28692300, PubMed:33823587).
The SEC pathway plays an important role for fungal soil colonization via decreasing fungal nematode-capturing ability (PubMed:33823587).
Within the pathway, the cytochrome P450 monooxygenase AOL_s00215g274 is involved in specific regional ketone reductions at C-4 of farnesyl epoxy-quinone (PubMed:28692300, PubMed:33823587).
The pathway begins with the biosynthesis of 6-methylsalicylic acid (6-MSA), the first precursor of the polyketide-derived epoxycyclohexenol in arthrosporols, by the polyketide synthase (PKS) AOL_s00215g283 via condensation of 1 acetate and 3 malonate units. The 6-methylsalicylic acid decarboxylase AOL_s00215g281 then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol. The cytochrome P450 monooxygenase AOL_s00215g282 further oxidizes m-cresol to yield toluquinol. With the assistance of the oxidoreductase AOL_s00215g277, the polyprenyl transferase AOL_s00215g276 catalyzes the farnesylation of toluquinol to produce farnesyl hydroquinone, the hybrid precursor for biosynthesis of SECs. Farnesyl hydroquinone undergoes epoxidation and then subsequent dehydrogenation to form farnesyl epoxy-quinone, the first and simplest SEC. The cytochrome P450 monooxygenase AOL_s00215g278 and the FAD-dependent monooxygenase AOL_s00215g279 might be involved in the oxygenation of the phenol moiety, most likely in the epoxy formation. The cytochrome P450 monooxygenases AOL_s00215g274 and AOL_s00215g280 are involved in specific regional ketone reductions at respectively C-4 and C-1 of farnesyl epoxy-quinone PubMed:33823587 (Probable).
The SEC pathway plays an important role for fungal soil colonization via decreasing fungal nematode-capturing ability (PubMed:33823587).
Within the pathway, the cytochrome P450 monooxygenase AOL_s00215g274 is involved in specific regional ketone reductions at C-4 of farnesyl epoxy-quinone (PubMed:28692300, PubMed:33823587).
The pathway begins with the biosynthesis of 6-methylsalicylic acid (6-MSA), the first precursor of the polyketide-derived epoxycyclohexenol in arthrosporols, by the polyketide synthase (PKS) AOL_s00215g283 via condensation of 1 acetate and 3 malonate units. The 6-methylsalicylic acid decarboxylase AOL_s00215g281 then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol. The cytochrome P450 monooxygenase AOL_s00215g282 further oxidizes m-cresol to yield toluquinol. With the assistance of the oxidoreductase AOL_s00215g277, the polyprenyl transferase AOL_s00215g276 catalyzes the farnesylation of toluquinol to produce farnesyl hydroquinone, the hybrid precursor for biosynthesis of SECs. Farnesyl hydroquinone undergoes epoxidation and then subsequent dehydrogenation to form farnesyl epoxy-quinone, the first and simplest SEC. The cytochrome P450 monooxygenase AOL_s00215g278 and the FAD-dependent monooxygenase AOL_s00215g279 might be involved in the oxygenation of the phenol moiety, most likely in the epoxy formation. The cytochrome P450 monooxygenases AOL_s00215g274 and AOL_s00215g280 are involved in specific regional ketone reductions at respectively C-4 and C-1 of farnesyl epoxy-quinone PubMed:33823587 (Probable).
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | oxidoreductase activity | |
Biological Process | terpenoid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameShort chain dehydrogenase AOL_s00215g274
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Orbiliomycetes > Orbiliales > Orbiliaceae > Orbilia > Orbilia oligospora
Accessions
- Primary accessionG1XTZ5
Proteomes
Phenotypes & Variants
Disruption phenotype
Abolishes the production of arthrobotrisins A to D and arthrosporol A, and leads to the accumulation of 11 new sesquiterpenyl epoxy-cyclohexenoids (SECs) and derivatives with diverse oxidation patterns (PubMed:28692300, PubMed:33823587).
Shows substantial reduction in conidiation (PubMed:33823587).
Develops far more adhesive trapping devices and traps and increases the number of captured nematodes by the traps (PubMed:33823587).
Shows significantly increased ammonia levels in fungal mycelia (PubMed:33823587).
Shows substantial reduction in conidiation (PubMed:33823587).
Develops far more adhesive trapping devices and traps and increases the number of captured nematodes by the traps (PubMed:33823587).
Shows significantly increased ammonia levels in fungal mycelia (PubMed:33823587).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000457842 | 1-322 | Short chain dehydrogenase AOL_s00215g274 | |||
Sequence: MAPRIPSIPSSTDLSGQSALVTGSNTGIGFENARQFLQLKASPVYLAVRSVERGQEAKKLLLDDPEVKKKNPGAVVEIYQVDMASFDSVAAFAQKFSEVKKLNIAVLNAGVSFFKYIPTSDGYETVLQVNYLSNALLATHLLPLLKAGAAASGKPSHLAFVSSNMQHMTSLKKNTIKPNENIIDWFNNRANFGMDRYNVSKLLLTGFTNELASKIDSSQVVINSMCPGLVATNFDTNSPWYLKYLMKGVRSLMARTPSEGARALTLAAITGTEGNGKYYSDGKETPSAALLLTEDGKAFQKKLWDQTLERIQQLDPTSPPPI |
Expression
Induction
Expression is down-regulated by the cluster protein AOL_s00215g275.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length322
- Mass (Da)35,058
- Last updated2011-11-16 v1
- Checksum427DD189BFB2F764
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ADOT01000316 EMBL· GenBank· DDBJ | EGX43538.1 EMBL· GenBank· DDBJ | Genomic DNA |