H1VQW0 · DPCHF_COLHI
- ProteinFAD-dependent oxidoreductase dpchF
- GenedpchF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids473 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
FAD-dependent oxidoreductase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B (PubMed:32286350).
The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin B (PubMed:32286350).
Finally, the FAD-dependent oxidoreductase dpchF converts higginsianin B into higginsianin A (PubMed:32286350).
The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin B (PubMed:32286350).
Finally, the FAD-dependent oxidoreductase dpchF converts higginsianin B into higginsianin A (PubMed:32286350).
Cofactor
Biotechnology
Diterpenoid pyrones display various biological activities and higginsianin A shows anti-HIV activity.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
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 nameFAD-dependent oxidoreductase dpchF
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Glomerellaceae > Colletotrichum > Colletotrichum destructivum species complex
Accessions
- Primary accessionH1VQW0
Proteomes
Organism-specific databases
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MKLSFIASPVWALALAQFAAA | ||||||
Chain | PRO_5010497735 | 22-473 | FAD-dependent oxidoreductase dpchF | |||
Sequence: TQVKIDVDVAIFGGGSAGIHAAIQLRDAGATVAVIEKKSQIGGHAETYTDPQGKSTNVGVVVFDNIEVASNYFARLNVSIVRGSPLGTAGPTYTYDFTSGAQIPAVNTSAEAQQQLTAALQSYSTNVLSKYPWIDEGFLVPDPVPEELTIPFGELAQKYNFTALMPTIAMYNYFTGDLSTIPSLYGIKGLGQGALKNLFGSFILPASGKTRDLYDAAAIELGNSVLLNADVVKVQRDVRINSTTTGVTVLIQQPGQPPKLIRARKLLVAAPPTLENVGAFDLTAEERGLISKFSSLGCWASVANVPGLNVTLKNYGVHMPYNQPSIPGPYGFVAYGSPNNFLVTVGLPDAANTAAKGEAVVRQSLATLSAVGAVPADALEKLTFPFSAVHSPYSLRVSAEEIKAGFYSKFLALEGARNTYWTGAVWAGHNSALIWNFNMGTVLPGLKKDLGL | ||||||
Glycosylation | 98 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 128 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 181 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 262 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 330 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length473
- Mass (Da)50,041
- Last updated2012-03-21 v1
- ChecksumF55B664135600AC4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LTAN01000004 EMBL· GenBank· DDBJ | OBR09790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CACQ02005519 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |