A0JJU0 · TENC_BEABA
- ProteinTrans-enoyl reductase tenC
- GenetenC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids388 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection (PubMed:17216664, PubMed:18266306, PubMed:20575135, PubMed:34903054).
TenC collaborates with the hybrid PKS-NRPS synthetase tenS to catalyze the assembly of the polyketide-amino acid backbone, since tenS lacks a designated enoylreductase (ER) domain (PubMed:18266306, PubMed:34903054).
Upon formation of the polyketide backbone on the thiotemplate of tenS, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D (PubMed:18266306, PubMed:34903054).
The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined (PubMed:34903054).
TenC collaborates with the hybrid PKS-NRPS synthetase tenS to catalyze the assembly of the polyketide-amino acid backbone, since tenS lacks a designated enoylreductase (ER) domain (PubMed:18266306, PubMed:34903054).
Upon formation of the polyketide backbone on the thiotemplate of tenS, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D (PubMed:18266306, PubMed:34903054).
The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined (PubMed:34903054).
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 51-54 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 142-149 | substrate | |||
Binding site | 219-222 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 237 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 284-285 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 304-308 | substrate | |||
Binding site | 373-374 | 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 tenC
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Cordycipitaceae > Beauveria
Accessions
- Primary accessionA0JJU0
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000438446 | 1-388 | Trans-enoyl reductase tenC | ||
Expression
Induction
Expression is positively regulated by the cluster-specific transcription factor tenR and is induced during cocultures with the natural competitor fungus Metarhizium robertsii.
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length388
- Mass (Da)41,318
- Last updated2006-12-12 v1
- MD5 Checksum6156586D54675A79F93014D2526348E5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM409327 EMBL· GenBank· DDBJ | CAL69596.1 EMBL· GenBank· DDBJ | Genomic DNA |