A0A166YZU9 · PPZE_METRR
- ProteinCytochrome P450 monooxygenase ppzE
- GeneppzE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids392 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity (PubMed:30452111).
The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine (PubMed:30452111).
The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine (By similarity).
The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine (By similarity).
The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase (By similarity).
Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine (By similarity).
This final oxidation to give the pyrrole functionality may be spontaneous (By similarity).
In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium rileyi that contains additional pyrrolopyrazine biosynthesis genes (Probable). The 2-oxoglutarate-Fe(II) type oxidoreductases ppzC and ppzD could be candidates for conversion of proline into an oxidized derivative to be used by the ppzA A1-domain as substrate (Probable). The other ppz genes encode proteins predicted to derivatize peramine into more complex pyrrolopyrazine metabolites (Probable)
The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine (PubMed:30452111).
The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine (By similarity).
The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine (By similarity).
The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase (By similarity).
Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine (By similarity).
This final oxidation to give the pyrrole functionality may be spontaneous (By similarity).
In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium rileyi that contains additional pyrrolopyrazine biosynthesis genes (Probable). The 2-oxoglutarate-Fe(II) type oxidoreductases ppzC and ppzD could be candidates for conversion of proline into an oxidized derivative to be used by the ppzA A1-domain as substrate (Probable). The other ppz genes encode proteins predicted to derivatize peramine into more complex pyrrolopyrazine metabolites (Probable)
Cofactor
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
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 ppzE
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Metarhizium
Accessions
- Primary accessionA0A166YZU9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 10-30 | Helical | ||||
Sequence: LELVWFVALYPFACWTLFAVL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450263 | 1-392 | Cytochrome P450 monooxygenase ppzE | |||
Sequence: MLSIIHVGWLELVWFVALYPFACWTLFAVLKSVYRITLHPLAKFPGPKLAGASYCYEFWYEIVCGIQYTQKIIKLHEQYGPIVRINPDELHFNDIDFVDVVYTAGARKRDKSRHYLAGFEGSIIRFVSSDFHSFLIDTRVKKPERLKRVVLGAERHHDAKDCPMFLELLNSNLPAQEKSKQRLMYEANGATLAGSGSTAIALSNIVYNLVANPRIGHKLRSELMRKVSASKNLPTWSTLEELPYLTAVIHEGLRSMYDPSKERLPYDPSQERLPRVATEEELIYEGGSALGKSKYVIPRGYAISTSAHVVHSDESIFPNASQFDPERWLDRDGQRNKELERHLLSFSKGSRHCLGMHCRRATCLAIPASARNGTSGYQFTSGQLEYKVQERQ | ||||||
Glycosylation | 319 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 372 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length392
- Mass (Da)44,641
- Last updated2016-07-06 v1
- Checksum7AAF7E1ECA7CDBC5
Keywords
- Technical term