A0JJT9 · TENB_BEABA

Function

function

Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection (PubMed:17216664, PubMed:19067514, PubMed:20575135, PubMed:34903054).
TenB catalyzes the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively (PubMed:19067514, PubMed:34903054).
The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined (PubMed:34903054).

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site481Fe (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 tenB
  • EC number
  • Alternative names
    • Tenellin biosynthesis protein B

Gene names

    • Name
      tenB
    • Synonyms
      ORF2

Organism names

Accessions

  • Primary accession
    A0JJT9
  • Secondary accessions
    • E2GC97

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane13-33Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Fails to produce tenellin, and accumulates pretenellin B (PubMed:19067514).
Leads also to the accumulation of pyridovericin (PubMed:34903054).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004384521-539Cytochrome P450 monooxygenase tenB

Expression

Induction

Expression is positively regulated by the cluster-specific transcription factor tenR and is induced during cocultures with the natural competitor fungus Metarhizium robertsii.

Structure

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias439-458Basic and acidic residues
Region439-460Disordered

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    539
  • Mass (Da)
    61,065
  • Last updated
    2006-12-12 v1
  • Checksum
    FDCF0430D15A2C82
MALFQAMSMVAQLGYYEKVAGVLGFLSIALLFWKLNHKPFYPALPLAGEPPQRRWFSLSNRLRYYNDCAALFDEAYHTAYAKKGKAVLVPSMGVHTAMIMPESAMNWAMSQPDDSLSIKKAFSELNQTKYSLGHGRYWEDPWQLDLVKAHLSSILQNLIPQLNEELAAAFSKHLGTDAENWKEIELEVIMRRIIAQATSRFIVGLPLCRDDGYLDLSYKVILGMVTTIWATLPFPDLIRAITGPIASWQTRRNIARIQEYLEPLYQERISILESRDGPESDPEPQDLFMMMLRFAQKKRPDEYANLGIMTRRVCAANFVAMHQSTVSVTNLILNIIGSDAEFNTTATLRDEITQVMRGTDAKSWTKDTFTRMRKCDSVAREAMRLNFPLGTRGSMRAVLKDGLESPEGIKLQKGTTISWLASCAQVDADRFDNPQKFDPFRFSRASKDDDDDGKSTSSHAKDAFVTTSPQYLPFGHGKHACPGRFMVDLMFKILLAQLLTHYDLGWPEDYQGKQPPSVWQGELSEPPPGARILVKRRKV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias439-458Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HM243222
EMBL· GenBank· DDBJ
ADN43683.1
EMBL· GenBank· DDBJ
Genomic DNA
AM409327
EMBL· GenBank· DDBJ
CAL69595.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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