J5JKC1 · TENA_BEAB2
- ProteinCytochrome P450 monooxygenase tenA
- GenetenA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids529 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Cytochrome P450 monooxygenase; 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:19067514, PubMed:20575135, PubMed:34903054).
TenA catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to the production of pretenellin B and pyridovericin, respectively (PubMed:19067514, 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).
TenA catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to the production of pretenellin B and pyridovericin, respectively (PubMed:19067514, 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).
Cofactor
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 477 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | monooxygenase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome P450 monooxygenase tenA
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Cordycipitaceae > Beauveria
Accessions
- Primary accessionJ5JKC1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 8-24 | Helical | |||
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Fails to produce tenellin, and leads to the accumulation of 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000455688 | 1-529 | Cytochrome P450 monooxygenase tenA | ||
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
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length529
- Mass (Da)60,680
- Last updated2012-10-31 v1
- MD5 Checksum6BD20154E52A36425531918ED50C3E2A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JH725173 EMBL· GenBank· DDBJ | EJP63691.1 EMBL· GenBank· DDBJ | Genomic DNA |