A0A1B7YCL6 · DPCHH_COLHI
- ProteinShort chain dehydrogenase/reductase dpchH
- GenedpchH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids401 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Short chain dehydrogenase/reductase; 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).
Biotechnology
Diterpenoid pyrones display various biological activities and higginsianin A shows anti-HIV activity.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 72-80 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: KKSLSGFGD | ||||||
Binding site | 99-100 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 118-120 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: AKV | ||||||
Active site | 275 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 275-279 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: YGTSK | ||||||
Binding site | 308-310 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GTI |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
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/reductase dpchH
- 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 accessionA0A1B7YCL6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 51-71 | Helical | ||||
Sequence: VRAVDVLFGTFLYVPLGILFL |
Keywords
- Cellular component
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451553 | 1-401 | Short chain dehydrogenase/reductase dpchH | |||
Sequence: MWTGQPASGPPFDHENHSASCTQHFALFSSPSPANSEPKSMLSAWAHRLCVRAVDVLFGTFLYVPLGILFLKKSLSGFGDGDWDSSQIPDLHGKVAVVTGGNAGIGYHTVRQLAAKGAKVYLAARSESRAKEAIKRLREENPDIPQEKLVWLPLDLSSQAQVVDAARDLMSKTERLDILVNNAGVDPYNYVKTADGFEMTMAVNHIGHWTLTYCLLPLLKATAAQQGSDVRVITLSSSGERNHSANNHFTTLKDLDDPCAGPGWEDSRLAQGKRYGTSKLANILFATELQRRMDEEGAGILSLSLNPGTIRTEGAADVMPLVTQPLVWLLFTDAAKGADTTMFAATAREVRENSEQWKGRYLDGPGRIKPPSPKARDAVAARNLWNITAAAVKGTGALEKL | ||||||
Glycosylation | 16 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 242 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 386 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length401
- Mass (Da)43,505
- Last updated2016-11-02 v1
- Checksum8D9FA383AE9D62D8
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM004458 EMBL· GenBank· DDBJ | OBR09787.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CACQ02005368 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |