Q0UI04 · ELCD_PHANO

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).

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site269S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site319Proton acceptor

GO annotations

AspectTerm
Molecular FunctionO-methyltransferase activity
Biological Processbiosynthetic process
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    O-methyltransferase elcB
  • EC number
  • Alternative names
    • Elsinochrome C biosynthesis cluster protein D

Gene names

    • Name
      elcD
    • ORF names
      SNOG_08610

Organism names

Accessions

  • Primary accession
    Q0UI04

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004498551-437O-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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    437
  • Mass (Da)
    48,108
  • Last updated
    2006-09-05 v1
  • Checksum
    91AC8091485FB6D5
MSLLQLTASITKAAADLDDATNNAAKASEIESKAKTALLDAAERLVLAYRSPRQWLIDLSFQHCATASLQMIMKYRLHHAVPKQGSRSFAEIAEIITTPDQPGKLPESLVGRLLQHAMSFGLFTPAASGRVAHNDASLLLVTDPDLEAWVYLCSNVAYPAGAQLPKAIEQYGASSEPSETAYSVSIGRRISQFERFREPDGHAEHEMFARAMKGISAGGAYDVGHVVDGGYPWHELPEGTLVVDVGGGPGHVAIALARKYPQLLFEVQDLVETVEFGAKNCPKDLQHRVSFRAQDFFKPQPQRETDSRTIVYFARFILHDWSDKYAGQIVEPLAQAMRPQDRLILNEVVVPEPSVEQRIERKSHDRDLLMLMNLNGRERTLVAFEGLFEVVSPRLRVEKVHKPTTGGELSLITASVDKLTGRKSAGGDIFGANVDEA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH445337
EMBL· GenBank· DDBJ
EAT83778.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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