A0A3Q9U4Z5 · PVHC_TALVA
- ProteinTrans-enoyl reductase pvhC
- GenepvhC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids358 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
function
Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of varicidin A, an antifungal natural product containing a cis-octahydrodecalin core (PubMed:30609896).
The PKS module of pvhA together with the enoylreductase pvhC catalyze the formation of the polyketide unit which is then conjugated to L-isoleucine by the condensation domain of the NRPS module (PubMed:30609896).
Activity of the Dieckmann cyclase domain (RED) of pvhA results in release of an acyclic tetramate (PubMed:30609896).
The cytochrome P450 monooxygenase pvhE then catalyzes the oxidation of the C21 methyl group to a to carboxylate group (PubMed:30609896).
The methyltransferase pvhD then further methylates the pvhE product (PubMed:30609896).
The Diels-Alderase pvhB is able to catalyze Diels-Alder cycloaddition using both pvhE and pvhD products as substrates to form the decalin ring, yielding varicidin B and A, respectively (PubMed:30609896).
The PKS module of pvhA together with the enoylreductase pvhC catalyze the formation of the polyketide unit which is then conjugated to L-isoleucine by the condensation domain of the NRPS module (PubMed:30609896).
Activity of the Dieckmann cyclase domain (RED) of pvhA results in release of an acyclic tetramate (PubMed:30609896).
The cytochrome P450 monooxygenase pvhE then catalyzes the oxidation of the C21 methyl group to a to carboxylate group (PubMed:30609896).
The methyltransferase pvhD then further methylates the pvhE product (PubMed:30609896).
The Diels-Alderase pvhB is able to catalyze Diels-Alder cycloaddition using both pvhE and pvhD products as substrates to form the decalin ring, yielding varicidin B and A, respectively (PubMed:30609896).
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 48-51 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 134-141 | substrate | |||
Binding site | 169-172 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 192-195 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 210 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 257-258 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 278-282 | substrate | |||
Binding site | 347-348 | NADP+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | nucleotide binding | |
Molecular Function | oxidoreductase activity, acting on NAD(P)H |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTrans-enoyl reductase pvhC
- EC number
- Short namesER pvhC
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Trichocomaceae > Talaromyces
Accessions
- Primary accessionA0A3Q9U4Z5
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000453337 | 1-358 | Trans-enoyl reductase pvhC | ||
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length358
- Mass (Da)38,438
- Last updated2019-04-10 v1
- Checksum915F332F1B336453
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MK376933 EMBL· GenBank· DDBJ | AZZ09612.1 EMBL· GenBank· DDBJ | Genomic DNA |