P9WEU0 · ILID_HYPJQ
- ProteinS-adenosyl-L-methionine-dependent Diels-Alderase iliD
- GeneiliD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids305 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
S-adenosyl-l-methionine-dependent Diels-Alderase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:34947016).
IliD catalyzes the Diels-Alder reaction that converts the acyclic 2-pyridone intermediate to 8-epi-ilicicolin H (PubMed:34947016).
The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable) (PubMed:34947016).
IliD catalyzes the Diels-Alder reaction that converts the acyclic 2-pyridone intermediate to 8-epi-ilicicolin H (PubMed:34947016).
The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable) (PubMed:34947016).
Catalytic activity
- 3-[(2E,4E,8S,10E,12Z)-4,8-dimethyltetradeca-2,4,10,12-tetraenoyl]-4-hydroxy-5-(4-hydroxyphenyl)-1,2-dihydropyridin-2-one = ilicicolin HThis reaction proceeds in the forward direction.
Cofactor
Pathway
Mycotoxin biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | S-adenosylmethionine-dependent methyltransferase activity | |
Biological Process | organic hydroxy compound biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameS-adenosyl-L-methionine-dependent Diels-Alderase iliD
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionP9WEU0
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000455714 | 1-305 | S-adenosyl-L-methionine-dependent Diels-Alderase iliD | |||
Sequence: MSSTQTTAAEPIMTDNVALRAYYESWDSRVVYQIIMGGTQHFGYWDKDTYWPFPLGSKLRRSMEQKLMEILALPKGSRVLDAGCGVGHVARYMAQHGMRVFGIDIIDWAIEDARKAAKDAGLSKEMMSVEKMDYHHLDSLASESFDGVYTMQAFGHAVDPQKAMAGFFRVVRPGGRIAMVEVERKTAAKHDDPNDRLTQELKMVNDYTVMPTNEAASEDYFKNLLEEAGFVDVVVRDWQPNILPILRLFYSLVMIPYLFFRLFGNEKSFINMICARSGYAGRSRWRFVAITATKAGEKLEDHKSK |
Family & Domains
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length305
- Mass (Da)34,700
- Last updated2022-08-03 v1
- Checksum5FB02C2F1DA40120
Keywords
- Technical term