Q6WP51 · BOT3_BOTFU

Function

function

Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of botrydial (PubMed:14651630, PubMed:19035644, PubMed:27529428).
Botrydial is necessary for colonization of plant tissue by the T4 strain (PubMed:19035644).
It is a strain-dependent virulence factor since highly aggressive strains like SAS56 or B05 still retain substantial virulence when botrydial synthesis is impaired, since they produce also botcinic acid (PubMed:15986930).
The first step of botrydial biosynthesis is performed by the sesquiterpene synthase BOT2 which catalyzes the cyclization of farnesyl diphosphate (FPP) to presilphiperfolan-8-beta-ol (PSP) (PubMed:19035644, PubMed:19476353).
The cytochrome P450 monooxygenase BOT4 then catalyzes the hydroxylation at C-4 to give a probotryane intermediate (PubMed:27529428, PubMed:28617493).
Acetylation of the hydroxyl at C-4 is carried out by the acetyltransferase BOT5, followed by the combined action of the P450 monooxygenases BOT3 and BOT1, to yield finally the glycol, via the regio- and stereospecific hydroxylations at C-10 and C-15 of the probotryane intermediates, respectively (PubMed:15986930, PubMed:27529428).
The cleavage of the C10-C15 bond of probotryane skeleton is an intriguing and chemically important reaction, which could be mediated by some of the monooxygenases or by a combination of them (PubMed:27529428).
It is possible that either BOT3 or BOT1 would oxidize either the 10- or the 15-hydroxy group to the hydroperoxide derivative, which would then undergo heterolytic fragmentation to give the dialdehyde botrydial (PubMed:27529428).
Finally, the dehydrogenase BOT7 might be involved in the conversion of botrydial to dihydrobotrydial (PubMed:27721016).

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site509Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionmonooxygenase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome P450 monooxygenase BOT3
  • EC number
  • Alternative names
    • Botrydial biosynthesis cluster protein 3
    • Calcineurin-dependent protein 11

Gene names

    • Name
      BOT3
    • Synonyms
      CND11

Organism names

Accessions

  • Primary accession
    Q6WP51

Subcellular Location

Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane68-88Helical
Transmembrane366-386Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Abolishes the production of botrydial and accumulates high levels of the biosynthetic intermediate beta-acetoxy-15-alpha--hydroxyprobotryane and small amounts of botcinin A (PubMed:27529428).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004446431-567Cytochrome P450 monooxygenase BOT3

Expression

Induction

The botrydial biosynthesis cluster genes are co-regulated by the Ca2+/calcineurin signal transduction pathway, which is under the control of the alpha subunit BCG1 of a heterotrimeric G protein (PubMed:14651630, PubMed:19035644).
Expression of the cluster is also positively regulated by the cluster-specific transcription factor BOT6 (PubMed:27721016).

Structure

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    567
  • Mass (Da)
    64,374
  • Last updated
    2004-07-05 v1
  • Checksum
    A6E9EFC2982681CA
MEKSNPTLDLATKTALLTWQKSNALLQHGIERATPFVLAVKSKAWQDAQSIGSKVAEAKFRDIDRTEITTITSVALGLYFAYVFCLVFYRLYLHPLAKFPGYRICAACEWYEFYCYIVKGGQWGNEIRKMHEKYGPIVRTSPWELSVRDPAFYDQLYVTASTRKTDMWPRGREGNGFDNSHHLSVSHELHRTRRKHLEPFFSRQGITRIESRIAERVMKMDDRLVGLKGSGSIIEVDHMLCALTGDIIGQVSSGMEAGLLDDPEFTPAWKDLMIKSTAIAPLFRCFPWINKFLQSLPTSIMNSVYPKGISNMMLGKTGQQNIEKIKTQIATSKRDLSDVSVFHHLLSSNVPESEKSIDRLRAESMILLLAGTLAGAHTLTFVVFYVLQNPQIEKRLRAELQPVFKGYPNKMPTWAELEKLPYLRGCVKEALRLNGLVGNLARCSPDEDIQFHQWVIPKKTPVGMSIYAMHFDQNVFSEPEAFKPERWIGEYNKQMDRNFVPFTKGSRSCLGVNLAWAELYLASAMLFRPGGPKLVLHDGGESDIKIARDYIMGFPKAGAKDVRVKIE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY277723
EMBL· GenBank· DDBJ
AAQ16574.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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