A0A166YZY9 · PPZC_METRR
- Protein2-oxoglutarate-Fe(II) type oxidoreductase ppzC
- GeneppzC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids374 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
2-oxoglutarate-Fe(II) type oxidoreductase; 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
Note: Binds 1 Fe2+ ion per subunit.
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | dioxygenase activity | |
Molecular Function | metal ion binding | |
Biological Process | small molecule biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-oxoglutarate-Fe(II) type oxidoreductase ppzC
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Metarhizium
Accessions
- Primary accessionA0A166YZY9
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450257 | 1-374 | 2-oxoglutarate-Fe(II) type oxidoreductase ppzC | |||
Sequence: MATDTAVTGAPETTELRLASGNGPVTRTVLRTPVRDALPSEVPLIDISPIFSTCVADRKAVARKIHDAATNIGFFYIQNHRVPSQDIDLAYSASQDFFRQEMEVKVEADAKDGPFDSGYRGPGTQRVNPTEGADLRETYSILYDPMLDPTVPDPANIPEPASRFLHLGRAPFESTATLPHFKDAFVRYFQACLVLARALTRAFALSLDLPESAFDGKVQYPDASLEINFYPPISTGHAVSAPGDADTRVSIGSHTDFLLFTILWQDSNGGLQVLNREGQWIRAIPVEGTFVVNIGDYLQRVTNDKYVSTVHRAQNFSGRERVSMPFFWGFGMHESCQVLRNCCGEDEKSKYDEVKCVDWVSRRLGNLFDLSDKG |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 111-130 | Disordered | ||||
Sequence: KDGPFDSGYRGPGTQRVNPT | ||||||
Domain | 220-330 | Fe2OG dioxygenase | ||||
Sequence: YPDASLEINFYPPISTGHAVSAPGDADTRVSIGSHTDFLLFTILWQDSNGGLQVLNREGQWIRAIPVEGTFVVNIGDYLQRVTNDKYVSTVHRAQNFSGRERVSMPFFWGF |
Sequence similarities
Belongs to the iron/ascorbate-dependent oxidoreductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length374
- Mass (Da)41,480
- Last updated2016-07-06 v1
- Checksum4B8FFDD0AB8B09F3
Keywords
- Technical term