C9K7I3 · AMT82_ALTAL
- ProteinAconitase AMT8-2
- GeneAMT8-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids843 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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).
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).
The CDCs are not essential for saprophytic growth but controls host-selective pathogenicity (PubMed:17990954).
Pathway
Mycotoxin biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 258-260 | substrate | ||||
Sequence: DSH | ||||||
Binding site | 450 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 513 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 516 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 536 | substrate | ||||
Sequence: R | ||||||
Binding site | 541 | substrate | ||||
Sequence: R | ||||||
Binding site | 712-713 | substrate | ||||
Sequence: SR |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | hydro-lyase activity | |
Molecular Function | iron-sulfur cluster binding | |
Molecular Function | metal ion binding | |
Biological Process | L-amino acid biosynthetic process | |
Biological Process | proteinogenic amino acid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAconitase AMT8-2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Pleosporineae > Pleosporaceae > Alternaria > Alternaria sect. Alternaria > Alternaria alternata complex
Accessions
- Primary accessionC9K7I3
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000444851 | 1-843 | Aconitase AMT8-2 | |||
Sequence: MAAYLFTCSILQTLSEAGKIEIAEDKLLHYLGELPGTPNGPVQLLENICTILEGQGRATHGNVIRHVLNIVVTEQELGGLGISGKSWEEVDEHTLHEIKFLTDAWLTAAESRAAARHLPQPLKQQDTRRLPMNLAEKILAHHAFSVPRRERVVAGDLLRVSIDWVIASELSWVGMKHSVTSLDMKPSAWRNDRFWLSGDHTVDPRTYHDKRVQALIKGLESAKRDLKMTENQGSNYTIMHTEFVRERAEPGMLVLGSDSHTCSAGAVSALAIGLGAGDVMAGLATGETWFKVPECIRINFTGQPAWYIGGKDVILSVLKQLKRNTYAAERIVEFGGAGAKLLSCDARFAISNMCTVRDPNDRPELKPTADDRSTSRNLVLLQAFLFPTVSLNRLSIAAGARYEGASYASTFEIDLGEVEPFIAIYPSPDQVCPVAERTGMRFDGCFIGACTTTEEDLVLAALVLEAGLKRGLTLEKGKRIVVPGSLPIVKNLRALGLLDIYKACGYEQPAPGCSLCLGIGADVAEAGSQWLSSQNRNFQNRMGRGAVGHICSAATVAASSFNMTLTDPCDLLNDVSETTFKEYLARCKVARGGSESKLAGGKQANNVQYIEPCLLGENARSAEGEVPALEAAAVSLDDARLGSINSRIYKLDDYVDTDALPQIIPAPACVGSPTDEMLGSHCFELTNPDFRDYVRSGHRVIVGGRAFGCGSSREEAPRALKGLGVQCVIARSFAFIFGRNMPNIGMLAIVLTDEAFYKAAQQGENIEVDVEGRVVHVAGQTFPFSLDDMELQLIRNRGLAASYQKLGSKVFAALCQKPAPLPISALADATLAQGGSIGRQMDW |
Structure
Sequence
- Sequence statusComplete
- Length843
- Mass (Da)91,266
- Last updated2009-11-24 v1
- Checksum4AFC3BB97E1AC771