C9K7I3 · AMT82_ALTAL

Function

function

Aconitase; part of the gene clusters that mediate the biosynthesis of AM-toxins, host-selective toxins (HSTs) causing Alternaria blotch on apple, a worldwide distributed disease (By similarity).
AM-toxins are cyclic depsipeptides containing the 3 residues 2-hydroxy-isovaleric acid (2-HIV), dehydroalanine, L-alanine which are common for all 3 AM-toxins I to III. The fourth precursor is L-alpha-amino-methoxyphenyl-valeric acid (L-Amv) for AM-toxin I, L-alpha-amino-phenyl-valeric acid (L-Apv) for AM-toxin II, and L-alpha-amino-hydroxyphenyl-valeric acid (L-Ahv) for AM-toxin III (Probable). AM-toxins have two target sites for affecting susceptible apple cells; they cause invagination of the plasma membrane and electrolyte loss and chloroplast disorganization (PubMed:22846083).
The non-ribosomal peptide synthetase AMT1 contains 4 catalytic modules and is responsible for activation of each residue in AM-toxin (PubMed:10875335).
The aldo-keto reductase AMT2 catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV), one of the precursor residues incorporated by AMT1 during AM-toxin biosynthesis, by reduction of its ketone to an alcohol (PubMed:15066029).
The cytochrome P450 monooxygenase AMT3 and the thioesterase AMT4 are also important for AM-toxin production, but their exact function within the AM-toxin biosynthesis are not known yet (PubMed:17990954).
Up to 21 proteins (including AMT1 to AMT4) are predicted to be involved in AM-toxin biosynthesis since their expression ishighly up-regulated in AM-toxin-producing cultures (PubMed:17990954).

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:17990954).
The CDCs are not essential for saprophytic growth but controls host-selective pathogenicity (PubMed:17990954).

Pathway

Mycotoxin biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site258-260substrate
Binding site450[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site513[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site516[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site536substrate
Binding site541substrate
Binding site712-713substrate

GO annotations

AspectTerm
Molecular Functionhydro-lyase activity
Molecular Functioniron-sulfur cluster binding
Molecular Functionmetal ion binding
Biological ProcessL-amino acid biosynthetic process
Biological Processproteinogenic amino acid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aconitase AMT8-2
  • EC number
  • Alternative names
    • AM-toxin biosynthesis protein 8-2

Gene names

    • Name
      AMT8-2

Organism names

Accessions

  • Primary accession
    C9K7I3

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004448511-843Aconitase AMT8-2

Structure

Family & Domains

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    843
  • Mass (Da)
    91,266
  • Last updated
    2009-11-24 v1
  • Checksum
    4AFC3BB97E1AC771
MAAYLFTCSILQTLSEAGKIEIAEDKLLHYLGELPGTPNGPVQLLENICTILEGQGRATHGNVIRHVLNIVVTEQELGGLGISGKSWEEVDEHTLHEIKFLTDAWLTAAESRAAARHLPQPLKQQDTRRLPMNLAEKILAHHAFSVPRRERVVAGDLLRVSIDWVIASELSWVGMKHSVTSLDMKPSAWRNDRFWLSGDHTVDPRTYHDKRVQALIKGLESAKRDLKMTENQGSNYTIMHTEFVRERAEPGMLVLGSDSHTCSAGAVSALAIGLGAGDVMAGLATGETWFKVPECIRINFTGQPAWYIGGKDVILSVLKQLKRNTYAAERIVEFGGAGAKLLSCDARFAISNMCTVRDPNDRPELKPTADDRSTSRNLVLLQAFLFPTVSLNRLSIAAGARYEGASYASTFEIDLGEVEPFIAIYPSPDQVCPVAERTGMRFDGCFIGACTTTEEDLVLAALVLEAGLKRGLTLEKGKRIVVPGSLPIVKNLRALGLLDIYKACGYEQPAPGCSLCLGIGADVAEAGSQWLSSQNRNFQNRMGRGAVGHICSAATVAASSFNMTLTDPCDLLNDVSETTFKEYLARCKVARGGSESKLAGGKQANNVQYIEPCLLGENARSAEGEVPALEAAAVSLDDARLGSINSRIYKLDDYVDTDALPQIIPAPACVGSPTDEMLGSHCFELTNPDFRDYVRSGHRVIVGGRAFGCGSSREEAPRALKGLGVQCVIARSFAFIFGRNMPNIGMLAIVLTDEAFYKAAQQGENIEVDVEGRVVHVAGQTFPFSLDDMELQLIRNRGLAASYQKLGSKVFAALCQKPAPLPISALADATLAQGGSIGRQMDW

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB525200
EMBL· GenBank· DDBJ
BAI44807.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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