Q0UI04 · ELCD_PHANO
- ProteinO-methyltransferase elcB
- GeneelcD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids437 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of elsinochrome C, a perelyenequinone phytotoxin structurally similar to cercosporin (PubMed:28251756, PubMed:30809363).
The first step of elsinochrome C biosynthesis is performed by the polyketide synthase elcA which catalyzes the formation of nor-toralactone (PubMed:28251756, PubMed:30809363).
The starter unit acyltransferase (SAT) domain of elcA initiates polyketide extension by the selective utilization of acetyl-CoA, which is elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain by successive condensations with six malonyl units introduced by the malonyl acyltransferase (MAT) domain (By similarity).
The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a trihydroxynaphthalene, which is thought to be delivered to the thioesterase (TE) domain for product release (By similarity).
The bifunctional enzyme elcB then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (PubMed:28251756, PubMed:30809363).
The next step in perylenequinone biosynthesis is an O-methylation at the nascent OH-6 of the elcB product performed by the O-methyltransferase elcD (PubMed:30809363).
The oxidative coupling of the two monomeric naphthol units in perylenequinone biosynthesis is catalyzed by the FAD-dependent monooxygenase elcE and the multicopper oxidase elcG (PubMed:30809363).
ElcG might catalyze the first intermolecular coupling in a regio- and stereo-selective manner via a phenol radical coupling mechanism and the elcE could forge the second C-C bond intramolecularly via a hydride transfer mechanism (PubMed:30809363).
The fasciclin domain-containing protein elcF might also play a role duting this step (Probable). The last piece of the puzzle in the biosynthesis of elsinochrome C is the additional annulation by enolate coupling to afford the dihydrobenzo(ghi)perylenequinone system, catalyzed by the FAD-dependent monooxygenase elcH (PubMed:30809363).
The first step of elsinochrome C biosynthesis is performed by the polyketide synthase elcA which catalyzes the formation of nor-toralactone (PubMed:28251756, PubMed:30809363).
The starter unit acyltransferase (SAT) domain of elcA initiates polyketide extension by the selective utilization of acetyl-CoA, which is elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain by successive condensations with six malonyl units introduced by the malonyl acyltransferase (MAT) domain (By similarity).
The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a trihydroxynaphthalene, which is thought to be delivered to the thioesterase (TE) domain for product release (By similarity).
The bifunctional enzyme elcB then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (PubMed:28251756, PubMed:30809363).
The next step in perylenequinone biosynthesis is an O-methylation at the nascent OH-6 of the elcB product performed by the O-methyltransferase elcD (PubMed:30809363).
The oxidative coupling of the two monomeric naphthol units in perylenequinone biosynthesis is catalyzed by the FAD-dependent monooxygenase elcE and the multicopper oxidase elcG (PubMed:30809363).
ElcG might catalyze the first intermolecular coupling in a regio- and stereo-selective manner via a phenol radical coupling mechanism and the elcE could forge the second C-C bond intramolecularly via a hydride transfer mechanism (PubMed:30809363).
The fasciclin domain-containing protein elcF might also play a role duting this step (Probable). The last piece of the puzzle in the biosynthesis of elsinochrome C is the additional annulation by enolate coupling to afford the dihydrobenzo(ghi)perylenequinone system, catalyzed by the FAD-dependent monooxygenase elcH (PubMed:30809363).
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 269 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Active site | 319 | Proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | O-methyltransferase activity | |
Biological Process | biosynthetic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameO-methyltransferase elcB
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Pleosporineae > Phaeosphaeriaceae > Parastagonospora
Accessions
- Primary accessionQ0UI04
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000449855 | 1-437 | O-methyltransferase elcB | ||
Expression
Induction
Expression is up-regulated during the late stage of P.nodorum wheat leaf infection and is controlled by the cluster specific transporter elcR.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length437
- Mass (Da)48,108
- Last updated2006-09-05 v1
- Checksum91AC8091485FB6D5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH445337 EMBL· GenBank· DDBJ | EAT83778.1 EMBL· GenBank· DDBJ | Genomic DNA |