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A0JJU0 · TENC_BEABA

Function

function

Trans-enoyl reductase; 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:18266306, PubMed:20575135, PubMed:34903054).
TenC collaborates with the hybrid PKS-NRPS synthetase tenS to catalyze the assembly of the polyketide-amino acid backbone, since tenS lacks a designated enoylreductase (ER) domain (PubMed:18266306, PubMed:34903054).
Upon formation of the polyketide backbone on the thiotemplate of tenS, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D (PubMed:18266306, 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).

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site51-54NADP+ (UniProtKB | ChEBI)
Binding site142-149substrate
Binding site219-222NADP+ (UniProtKB | ChEBI)
Binding site237NADP+ (UniProtKB | ChEBI)
Binding site284-285NADP+ (UniProtKB | ChEBI)
Binding site304-308substrate
Binding site373-374NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionnucleotide binding
Molecular Functionoxidoreductase activity, acting on NAD(P)H

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Trans-enoyl reductase tenC
  • EC number
  • Alternative names
    • Tenellin biosynthesis protein C

Gene names

    • Name
      tenC
    • Synonyms
      ORF3

Organism names

Accessions

  • Primary accession
    A0JJU0

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004384461-388Trans-enoyl reductase tenC

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

Subunit

Monomer.

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    388
  • Mass (Da)
    41,318
  • Last updated
    2006-12-12 v1
  • MD5 Checksum
    6156586D54675A79F93014D2526348E5
MAAISSPPLTQKALKVASPDTLHLVTDAPLPTLGQDDSVLIRVVCVAINPVDGKSAEMSPTPGATSGTDFAGIVVALHGDAKSRTETADTIKTGDRVMGFVFGNNPHVLGNGAFAEYVTLPRRFLWRVPDHMSLEAAASLPVGVASVGMALHYLRISMSSLLKAVSRSIAAPSASQPHDGAFDSDANVFILVYGGGTSTGAIAIQILKAAGFHPITCCSSESASRAKRLGAVATFDYQSATCGRDIRDYTNDSLTLAIDCLSESASMAICYEAMGSAGGRYVSLDPFPVRGCVRRSIVPDWICSFTQFGQSIPWAPPYNLDERPDDHRLAEEWYHLAQKLLDAELIEAPTLEIRSGGLLHVPEGVAAVKLGQIKRRKLVYHISEEALP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AM409327
EMBL· GenBank· DDBJ
CAL69596.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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