B6HJU5 · ROQR_PENRW
- ProteinCytochrome P450 monooxygenase roqR
- GeneroqR
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids511 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxins roquefortine C and meleagrin (PubMed:22118684, PubMed:23776469).
The first stage is catalyzed by the dipeptide synthase roqA which condenses histidine and tryptophan to produce histidyltryptophanyldiketopiperazine (HTD) (PubMed:22118684, PubMed:23776469).
HTD is then converted to roquefortine C through two possible pathways (PubMed:23776469).
In the first pathway, prenyltransferase roqD transforms HTD to the intermediate roquefortine D, which is in turn converted to roquefortine C by the cytochrome P450 monooxygenase roqR (PubMed:23776469).
In the second pathway, HTD is first converted to the intermediate dehydrohistidyltryptophanyldi-ketopiperazine (DHTD) by roqR which is then prenylated by roqD to form roquefortine C (PubMed:23776469).
Roquefortine C can be further transformed to meleagrin via three more reactions including oxydation to glandicolin A by roqM, which is further reduced to glandicoline B by roqO (PubMed:23776469).
Finally, glandicoline B is converted to meleagrin by the glandicoline B O-methyltransferase roqN (PubMed:22118684, PubMed:23776469).
More studies identified further branching and additional metabolites produced by the roquefortine/meleagrin cluster, including roquefortine F, roquefortine L, roquefortine M, roquefortine N and neoxaline (PubMed:24225953).
The first stage is catalyzed by the dipeptide synthase roqA which condenses histidine and tryptophan to produce histidyltryptophanyldiketopiperazine (HTD) (PubMed:22118684, PubMed:23776469).
HTD is then converted to roquefortine C through two possible pathways (PubMed:23776469).
In the first pathway, prenyltransferase roqD transforms HTD to the intermediate roquefortine D, which is in turn converted to roquefortine C by the cytochrome P450 monooxygenase roqR (PubMed:23776469).
In the second pathway, HTD is first converted to the intermediate dehydrohistidyltryptophanyldi-ketopiperazine (DHTD) by roqR which is then prenylated by roqD to form roquefortine C (PubMed:23776469).
Roquefortine C can be further transformed to meleagrin via three more reactions including oxydation to glandicolin A by roqM, which is further reduced to glandicoline B by roqO (PubMed:23776469).
Finally, glandicoline B is converted to meleagrin by the glandicoline B O-methyltransferase roqN (PubMed:22118684, PubMed:23776469).
More studies identified further branching and additional metabolites produced by the roquefortine/meleagrin cluster, including roquefortine F, roquefortine L, roquefortine M, roquefortine N and neoxaline (PubMed:24225953).
Cofactor
Biotechnology
The indole alkaloid meleagrin was shown to be a good candidate to control c-Met-dependent breast cancer proliferation, migration and invasion (PubMed:26692349).
Pathway
Alkaloid biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
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 | |
Biological Process | mycotoxin biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome P450 monooxygenase roqR
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium > Penicillium chrysogenum species complex
Accessions
- Primary accessionB6HJU5
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MSGYVLLTVQLAAVLLLVTLWRA | ||||||
Chain | PRO_5002845764 | 24-511 | Cytochrome P450 monooxygenase roqR | |||
Sequence: FRPNTRSNRVVSYIINVGNTPKIHQKNKADFHPRTNVEISPLVVPNLFDRWLNAHSDLPLSISRWRGKYQVPGGGERLPILTGADEIKAVFKDSGNHRKASNLNGGWVMGDLVGDGVGLISEGHWKRVHAVVSPPFTQKPTTYVPFVQSRISRHFSELYPEDEGGRTLRIKPAEDLKLLPFWVISDLLYGNLSPEMTEELLQITDLRTDVFRYAFKGGLSLFSISKIFYPDIRNKLHVFHTRWANFNRKAYQCALNRDDASACAIVTLYRAVEQGQITPTELMHTLDEALFANIDVTIGSFSWIPQFLAEDAALQSKLRKEISHARSDTAPESWVKYIGSNSTLLASCINESARLKPVTNYTYAQSMPTDRDVGGYRIPRGTFMVVDTNALNIWDDAWGSDKTSYRPQRFLEESRASFRYRFWRFGFGPRQCIAQALADTILKVLVAYTVENYELKSTGKSAANEEDAHKQGEAWFKVAEQGIILEAL | ||||||
Glycosylation | 364 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 373 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 383 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length511
- Mass (Da)57,767
- Last updated2008-12-16 v1
- ChecksumF2C2D2F86F487B78
Keywords
- Technical term