D7UPN2 · ACTS2_ALTAL

Function

function

Trans-enoyl reductase; 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 of ACTT2 could not be accomplished due to the high number of the copies identified in the genome, the high sequence identity among these copies of ACTT2 is likely an advantage for RNA silencing, because it allows knockdown of all copies of this gene simultaneously (PubMed:18986255).

Pathway

Mycotoxin biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site42-45NADP+ (UniProtKB | ChEBI)
Binding site128-135substrate
Binding site162-165NADP+ (UniProtKB | ChEBI)
Binding site185-188NADP+ (UniProtKB | ChEBI)
Binding site203NADP+ (UniProtKB | ChEBI)
Binding site268-272substrate
Binding site333-334NADP+ (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 ACTTS2
  • EC number
  • Alternative names
    • ACT-toxin biosynthesis protein S2

Gene names

    • Name
      ACTTS2

Organism names

Accessions

  • Primary accession
    D7UPN2

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Targeted gene disruption leasd to a reduction in ACT-toxin production and pathogenicity, and transcriptional knockdown of ACTTS2 using RNA silencing results in complete loss of ACT-toxin production and pathogenicity (PubMed:20055645).
Does not affect growth rate, spore formation, and spore germination (PubMed:20055645).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004448641-343Trans-enoyl reductase ACTTS2

Interaction

Subunit

Monomer.

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    343
  • Mass (Da)
    36,508
  • Last updated
    2010-10-05 v1
  • MD5 Checksum
    92D1B6940C3D6D3DC654B8D595B34442
MLTRRALVVQSQGEVQVEEIPLPTLRDEYITVKVKAVALNPGDWKMLYGPHATPGSILGCDYSGVVEKVGRAVNALLTPGDRVAGFAFGGCPYNHDEGGFASYVTAKGDIQAKLSDSISFEDAATLGVGITTVGQAMYQALGLPLPPAIIQEAASILVYGASTATGTLAVQYAKLTGLKVFATASPHNFDLLKKLGADEVFDYRDPECGAKIRTVTNGLLSLVFDTISEGSSPAIWAAAMGAKGGKYTALLPIKNFPRSDVKVTTILGYTALGVKVSDHLPANQKDFEFSAKFWKLSQHLLEKEKIKTHPVGVRQGGIDAIPQGLQDLKNGRVSGVKLVYKID

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB510353
EMBL· GenBank· DDBJ
BAJ09790.1
EMBL· GenBank· DDBJ
Genomic DNA
AB516322
EMBL· GenBank· DDBJ
BAJ14523.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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