B6HJU5 · ROQR_PENRW

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).

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

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.

TypeIDPosition(s)Description
Binding site455Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionmonooxygenase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Biological Processmycotoxin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome P450 monooxygenase roqR
  • EC number
  • Alternative names
    • Roquefortine/meleagrin synthesis protein R

Gene names

    • Name
      roqR
    • ORF names
      Pc21g15470

Organism names

Accessions

  • Primary accession
    B6HJU5

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Leads to a reduction of both roquefortine C and meleagrin synthesis (PubMed:22118684, PubMed:23776469).
Accumulates HTD and roquefortine D (PubMed:23776469).

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_500284576424-511Cytochrome P450 monooxygenase roqR
Glycosylation364N-linked (GlcNAc...) asparagine
Glycosylation373N-linked (GlcNAc...) asparagine
Glycosylation383N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    511
  • Mass (Da)
    57,767
  • Last updated
    2008-12-16 v1
  • Checksum
    F2C2D2F86F487B78
MSGYVLLTVQLAAVLLLVTLWRAFRPNTRSNRVVSYIINVGNTPKIHQKNKADFHPRTNVEISPLVVPNLFDRWLNAHSDLPLSISRWRGKYQVPGGGERLPILTGADEIKAVFKDSGNHRKASNLNGGWVMGDLVGDGVGLISEGHWKRVHAVVSPPFTQKPTTYVPFVQSRISRHFSELYPEDEGGRTLRIKPAEDLKLLPFWVISDLLYGNLSPEMTEELLQITDLRTDVFRYAFKGGLSLFSISKIFYPDIRNKLHVFHTRWANFNRKAYQCALNRDDASACAIVTLYRAVEQGQITPTELMHTLDEALFANIDVTIGSFSWIPQFLAEDAALQSKLRKEISHARSDTAPESWVKYIGSNSTLLASCINESARLKPVTNYTYAQSMPTDRDVGGYRIPRGTFMVVDTNALNIWDDAWGSDKTSYRPQRFLEESRASFRYRFWRFGFGPRQCIAQALADTILKVLVAYTVENYELKSTGKSAANEEDAHKQGEAWFKVAEQGIILEAL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AM920436
EMBL· GenBank· DDBJ
CAP96444.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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