A0A1B7YCK2 · DPCHC_COLHI
- ProteinPolyprenyl transferase dpchC
- GenedpchC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids316 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Polyprenyl transferase; 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 | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | transferase activity, transferring alkyl or aryl (other than methyl) groups | |
Biological Process | terpenoid biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePolyprenyl transferase dpchC
- 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 accessionA0A1B7YCK2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 24-44 | Helical | ||||
Sequence: PLFTTFAGLWSTLLAGGAKMA | ||||||
Transmembrane | 60-80 | Helical | ||||
Sequence: ALCFVASYLFCGAGMVWNDWI | ||||||
Transmembrane | 105-125 | Helical | ||||
Sequence: EAMVWMVLQAALSWGVLEVML | ||||||
Transmembrane | 154-174 | Helical | ||||
Sequence: MLGIYPQYILAFTIAWPAVIG | ||||||
Transmembrane | 192-212 | Helical | ||||
Sequence: CLPLCTMVFFWTIYLNTAYSY | ||||||
Transmembrane | 234-254 | Helical | ||||
Sequence: IHLLLVALVSPILVCLPIYLF | ||||||
Transmembrane | 258-278 | Helical | ||||
Sequence: SLWLWLSWMGVWTASLAQQLV | ||||||
Transmembrane | 296-316 | Helical | ||||
Sequence: FILGIWTILACVVQVFLTGSA |
Keywords
- Cellular component
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451533 | 1-316 | Polyprenyl transferase dpchC | |||
Sequence: MAATKDRQLFRHLLRLSRFDRYNPLFTTFAGLWSTLLAGGAKMAEQRSDMSVATVFQQCALCFVASYLFCGAGMVWNDWIDRDIDANVARTKERPLASGKVTATEAMVWMVLQAALSWGVLEVMLDGKDVAKHFIPVAAASVLYPFGKRSLARMLGIYPQYILAFTIAWPAVIGRAAIYGQYESYAETLRQCLPLCTMVFFWTIYLNTAYSYQDVVDDRKLGVNSFYNIAGKHIHLLLVALVSPILVCLPIYLFELHSLWLWLSWMGVWTASLAQQLVQFDPKQPASGGSIHRSNFILGIWTILACVVQVFLTGSA |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length316
- Mass (Da)35,448
- Last updated2016-11-02 v1
- Checksum9EA58F0555BFF751
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LTAN01000004 EMBL· GenBank· DDBJ | OBR09786.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CACQ02005368 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |