C5NN19 · ACTT6_ALTAL

Function

function

Enoyl-CoA hydratase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) ACT-toxins responsible for brown spot of tangerine disease by the tangerine pathotype which affects tangerines and mandarins (PubMed:19271978).
ACT-toxins consist of three moieties, 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA), valine and a polyketide (PubMed:22846083).
ACT-toxin I is toxic to both citrus and pear; toxin II the 5''-deoxy derivative of ACT-toxin I, is highly toxic to pear and slightly toxic to citrus (PubMed:22846083).
On cellular level, ACT-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K+ after a few minutes of toxin treatment (PubMed:22846083).
The acyl-CoA ligase ACTT1, the hydrolase ACTT2, the enoyl-CoA hydratases ACTT3 and ACTT6, and the acyl-CoA synthetase ACTT5 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety (PubMed:18944496, PubMed:18986255, PubMed:19271978).
The exact role of each enzyme, and of additional enzymes identified within the AF-toxin clusters have still to be determined (PubMed:18944496, PubMed:18986255, PubMed:19271978).
On the other hand, ACTTS1 to ACTTS4 are specific to the tangerine pathotype (PubMed:22846083).
The function of ACTTS3 is to elongate the polyketide chain portion of ACT-toxin that is unique to this toxin (PubMed:20192828).
The enoyl-reductase ACTTS2 might complement the missing enoyl-reductase (ER) domain in ACTTS3 in the synthesis of the polyketide portion of ACT-toxin (PubMed:20055645).
The roles of the nonribosomal peptide synthetases-related proteins ACTTS1 and ACTTS4 have also still not been elucidated (PubMed:22846083).

Miscellaneous

Gene clusters encoding host-selective toxins (HSTs) are localized on conditionally dispensable chromosomes (CDCs), also called supernumerary chromosomes, where they are present in multiple copies (PubMed:18986255).
The CDCs are not essential for saprophytic growth but controls host-selective pathogenicity (PubMed:18986255).
Although conventional disruption could not be accomplished due to the high number of the copies identified in the genome, the high sequence identity among these copies is likely an advantage for RNA silencing, because it allows knockdown of all copies of this gene simultaneously (PubMed:18986255).

Pathway

Mycotoxin biosynthesis.

GO annotations

AspectTerm
Molecular Functionlyase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Enoyl-CoA hydratase ACTT6
  • EC number
  • Alternative names
    • ACT-toxin biosynthesis protein 6

Gene names

    • Name
      ACTT6

Organism names

Accessions

  • Primary accession
    C5NN19

Phenotypes & Variants

Disruption phenotype

Leads to drastic reduction of ACT-toxin production and disease severity after inoculation on detached leaves.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004448361-298Enoyl-CoA hydratase ACTT6

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    298
  • Mass (Da)
    32,631
  • Last updated
    2009-09-01 v1
  • MD5 Checksum
    29772CE4D1D89A991194F4BBC8DC1FB3
MTYFTIKSAAMSPDDDAPSPDINSLGRLMSHSEVESRGNGYEVLQQAGTVRILLSRPERGNALSLSLARDLTRLFQTFSAQHSVHRIVLTGKGKYFCSGMDLGEELYEDATERCLALQDLFGAIDACPKTTIAVINGPAFGGGVGLAFVCDIRVAVSTSFFCLSEVKLGLCPATVSRFIVREWGVSLARMAMLTARKIQPQTLHEMGVLHAVALDEEALEAVTRDVLNDLRFAAPQATAWCKVLTRKTRNANSDHDQLARQIFEAMVVAGSESEYGVAQFRLGNKNICWEQVECRHIG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB444614
EMBL· GenBank· DDBJ
BAH83503.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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