ID   AMT15_ALTAL             Reviewed;         157 AA.
AC   C9K7C7;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=AM-toxin biosynthesis protein 15 {ECO:0000303|PubMed:17990954};
GN   Name=AMT15 {ECO:0000303|PubMed:17990954};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND PATHWAY.
RC   STRAIN=NBRC 8984;
RX   PubMed=17990954; DOI=10.1094/mpmi-20-12-1463;
RA   Harimoto Y., Hatta R., Kodama M., Yamamoto M., Otani H., Tsuge T.;
RT   "Expression profiles of genes encoded by the supernumerary chromosome
RT   controlling AM-toxin biosynthesis and pathogenicity in the apple pathotype
RT   of Alternaria alternata.";
RL   Mol. Plant Microbe Interact. 20:1463-1476(2007).
RN   [2]
RP   FUNCTION.
RC   STRAIN=M-71;
RX   PubMed=10875335; DOI=10.1094/mpmi.2000.13.7.742;
RA   Johnson R.D., Johnson L., Itoh Y., Kodama M., Otani H., Kohmoto K.;
RT   "Cloning and characterization of a cyclic peptide synthetase gene from
RT   Alternaria alternata apple pathotype whose product is involved in AM-toxin
RT   synthesis and pathogenicity.";
RL   Mol. Plant Microbe Interact. 13:742-753(2000).
RN   [3]
RP   FUNCTION.
RC   STRAIN=NBRC 8984;
RX   PubMed=15066029; DOI=10.1111/j.1365-2958.2004.04004.x;
RA   Ito K., Tanaka T., Hatta R., Yamamoto M., Akimitsu K., Tsuge T.;
RT   "Dissection of the host range of the fungal plant pathogen Alternaria
RT   alternata by modification of secondary metabolism.";
RL   Mol. Microbiol. 52:399-411(2004).
RN   [4]
RP   REVIEW ON HOST-SELECTIVE TOXINS.
RX   PubMed=22846083; DOI=10.1111/j.1574-6976.2012.00350.x;
RA   Tsuge T., Harimoto Y., Akimitsu K., Ohtani K., Kodama M., Akagi Y.,
RA   Egusa M., Yamamoto M., Otani H.;
RT   "Host-selective toxins produced by the plant pathogenic fungus Alternaria
RT   alternata.";
RL   FEMS Microbiol. Rev. 37:44-66(2013).
CC   -!- FUNCTION: Part of the gene clusters that mediate the biosynthesis of
CC       AM-toxins, host-selective toxins (HSTs) causing Alternaria blotch on
CC       apple, a worldwide distributed disease (Probable). AM-toxins are cyclic
CC       depsipeptides containing the 3 residues 2-hydroxy-isovaleric acid (2-
CC       HIV), dehydroalanine, L-alanine which are common for all 3 AM-toxins I
CC       to III. The fourth precursor is L-alpha-amino-methoxyphenyl-valeric
CC       acid (L-Amv) for AM-toxin I, L-alpha-amino-phenyl-valeric acid (L-Apv)
CC       for AM-toxin II, and L-alpha-amino-hydroxyphenyl-valeric acid (L-Ahv)
CC       for AM-toxin III (Probable). AM-toxins have two target sites for
CC       affecting susceptible apple cells; they cause invagination of the
CC       plasma membrane and electrolyte loss and chloroplast disorganization
CC       (PubMed:22846083). The non-ribosomal peptide synthetase AMT1 contains 4
CC       catalytic modules and is responsible for activation of each residue in
CC       AM-toxin (PubMed:10875335). The aldo-keto reductase AMT2 catalyzes the
CC       conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric
CC       acid (2-HIV), one of the precursor residues incorporated by AMT1 during
CC       AM-toxin biosynthesis, by reduction of its ketone to an alcohol
CC       (PubMed:15066029). The cytochrome P450 monooxygenase AMT3 and the
CC       thioesterase AMT4 are also important for AM-toxin production, but their
CC       exact function within the AM-toxin biosynthesis are not known yet
CC       (PubMed:17990954). Up to 21 proteins (including AMT1 to AMT4) are
CC       predicted to be involved in AM-toxin biosynthesis since their
CC       expression ishighly up-regulated in AM-toxin-producing cultures
CC       (PubMed:17990954). {ECO:0000269|PubMed:10875335,
CC       ECO:0000269|PubMed:15066029, ECO:0000269|PubMed:17990954,
CC       ECO:0000303|PubMed:22846083, ECO:0000305|PubMed:10875335,
CC       ECO:0000305|PubMed:17990954}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:17990954}.
CC   -!- INDUCTION: Expression is up-regulated more than 10 fold in toxin
CC       producing cultures. {ECO:0000269|PubMed:17990954}.
CC   -!- MISCELLANEOUS: Gene clusters encoding host-selective toxins (HSTs) are
CC       localized on conditionally dispensable chromosomes (CDCs), also called
CC       supernumerary chromosomes, where they are present in multiple copies
CC       (PubMed:17990954). The CDCs are not essential for saprophytic growth
CC       but controls host-selective pathogenicity (PubMed:17990954).
CC       {ECO:0000269|PubMed:17990954}.
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DR   EMBL; AB525198; BAI44751.1; -; Genomic_DNA.
DR   EMBL; AB525199; BAI44774.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9K7C7; -.
PE   2: Evidence at transcript level;
KW   Virulence.
FT   CHAIN           1..157
FT                   /note="AM-toxin biosynthesis protein 15"
FT                   /id="PRO_0000444849"
FT   REGION          17..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   157 AA;  17981 MW;  F793F93CEFB0267C CRC64;
     MATLLCDLQE RSAKVERARH WDSKQGSSNS DVASGGSEVA GNSGNNSYLG DDVGWKIYPY
     RFLQLLQHLE QLQFTIQAPR HARLGISTVR MWSLRPYYNY DSYLEKDLIQ PDVPHDSLIW
     ALLRYVGRAV DRWVSRTFQP PRIRPLHAND PPAEASL