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J5JKC1 · TENA_BEAB2

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).
TenA catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to the production of pretenellin B and pyridovericin, 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 site477Fe (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 tenA
  • EC number
  • Alternative names
    • Tenellin biosynthesis protein A

Gene names

    • Name
      tenA
    • ORF names
      BBA_07335

Organism names

Accessions

  • Primary accession
    J5JKC1

Proteomes

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane8-24Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Fails to produce tenellin, and leads to the accumulation of 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004556881-529Cytochrome P450 monooxygenase tenA

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.

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
  • Length
    529
  • Mass (Da)
    60,680
  • Last updated
    2012-10-31 v1
  • MD5 Checksum
    6BD20154E52A36425531918ED50C3E2A
MLSLLDSVSLPYLILSACLSVILLRRFLAHDKGGSKSIAQGCLPEPRLRQWDPIFGFGIVISQARALRGHRYLEWLRDLHASMPHTKTFSANYGGYRWIFSIEPEILKAVYATNFQNFGVEPIRQHPPGFQPFAHKGVSTSDGDDWSFSRTLIKPFFERSVYVSTDRIKPFADKFMTLLPDDGETFDIQPLLQRWFLDITSEFIFGRSQDSMTHADRAEVTWAMADVLRGGRQRAQTHRILWAFNWDWWFEAVEKVHGFLNPYIRSTLKELEERQQRIKDGLPVDEERTDLLWSMATMLPDEEELRSQVCLIFVPNNDTTSMFIGHCLYFLARHSNAWKRLRDEVDAVGDAPITFEMLRNMKYLNGILNESMKPKPLSSKLTLALTTLCTPAHRLIPNNVTQVRAALSDVVLPLGGGPNGKAPLDVRKGDIVSVTKTVMYRDPDQWGPDANEYRPERWDGMRGGWHFLPYGGGPRRCPAQMMVQNESAYMLFRLAQKYSTIVARDPEPFRARMRIGPSSMHGVKIAFYK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JH725173
EMBL· GenBank· DDBJ
EJP63691.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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