A0A067XMP0 · PTAE_PESFW
- ProteinOxidoreductase ptaE
- GeneptaE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids610 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Oxidoreductase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:24302702).
The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA (PubMed:24302702).
As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain (PubMed:24302702).
The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrated to form endocrocin anthrone (PubMed:24302702).
Endocrocin anthrone is then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC (PubMed:24302702).
Spontaneous decarboxylation of endocrocin occurs to generate emodin (PubMed:24302702).
An O-methyltransferase (ptaH or ptaI) could methylate emodin to form physcion (PubMed:24302702).
PtaJ could then catalyze the oxidative cleavage of physcion, and rotation of the intermediate could then afford desmethylisosulochrin (PubMed:24302702).
PtaF, a putative NADH-dependent oxidoreductase, might also participate in the oxidative cleavage step (PubMed:24302702).
Desmethylisosulochrin is then transformed by another O-methyltransferase (ptaH or ptaI) to form isosulochrin (PubMed:24302702).
Chlorination of isosulochrin by ptaM in the cyclohexadienone B ring then produces chloroisosulochrin (PubMed:24302702).
PtaE is responsible for the oxidative coupling reactions of both benzophenones isosulouchrin and chloroisosulochrin to RES-1214-1 and pestheic acid respectively, regardless of chlorination
The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA (PubMed:24302702).
As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain (PubMed:24302702).
The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrated to form endocrocin anthrone (PubMed:24302702).
Endocrocin anthrone is then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC (PubMed:24302702).
Spontaneous decarboxylation of endocrocin occurs to generate emodin (PubMed:24302702).
An O-methyltransferase (ptaH or ptaI) could methylate emodin to form physcion (PubMed:24302702).
PtaJ could then catalyze the oxidative cleavage of physcion, and rotation of the intermediate could then afford desmethylisosulochrin (PubMed:24302702).
PtaF, a putative NADH-dependent oxidoreductase, might also participate in the oxidative cleavage step (PubMed:24302702).
Desmethylisosulochrin is then transformed by another O-methyltransferase (ptaH or ptaI) to form isosulochrin (PubMed:24302702).
Chlorination of isosulochrin by ptaM in the cyclohexadienone B ring then produces chloroisosulochrin (PubMed:24302702).
PtaE is responsible for the oxidative coupling reactions of both benzophenones isosulouchrin and chloroisosulochrin to RES-1214-1 and pestheic acid respectively, regardless of chlorination
Pathway
Secondary metabolite biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | copper ion binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOxidoreductase ptaE
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Xylariomycetidae > Xylariales > Sporocadaceae > Pestalotiopsis
Accessions
- Primary accessionA0A067XMP0
- Secondary accessions
Proteomes
Phenotypes & Variants
Disruption phenotype
Abolishes the production of pestheic acid and RES-1214-1, but accumulates isosulochrin and chloroisosulochrin (PubMed:24302702).
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-20 | ||||
Chain | PRO_0000443050 | 21-610 | Oxidoreductase ptaE | ||
Glycosylation | 105 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 111 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 262 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 277 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 330 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 356 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 401 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 409 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 427 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 602 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
PTM databases
Expression
Induction
The cluster is expressed in rice fermentation medium (PubMed:25623211).
Expression is correlated with the production of pestheic acid (PubMed:24302702).
Three regulators are located in the cluster (ptaR1, ptaR2 and ptaR3), suggesting that the production of pestheic acid is controlled by a complex regulatory mechanism (PubMed:24302702).
Expression is correlated with the production of pestheic acid (PubMed:24302702).
Three regulators are located in the cluster (ptaR1, ptaR2 and ptaR3), suggesting that the production of pestheic acid is controlled by a complex regulatory mechanism (PubMed:24302702).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 67-181 | Plastocyanin-like 1 | |||
Domain | 191-344 | Plastocyanin-like 2 | |||
Domain | 425-568 | Plastocyanin-like 3 | |||
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length610
- Mass (Da)68,758
- Last updated2018-01-31 v2
- ChecksumF5F87BE6DDD38970
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KC145148 EMBL· GenBank· DDBJ | AGO59042.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
KI912116 EMBL· GenBank· DDBJ | ETS76954.1 EMBL· GenBank· DDBJ | Genomic DNA |