ID   AMT12_ALTAL             Reviewed;         342 AA.
AC   C9K7C4;
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 12 {ECO:0000303|PubMed:17990954};
DE   Flags: Precursor;
GN   Name=AMT12 {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; BAI44748.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9K7C4; -.
PE   2: Evidence at transcript level;
KW   Signal; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..342
FT                   /note="AM-toxin biosynthesis protein 12"
FT                   /id="PRO_5002997608"
SQ   SEQUENCE   342 AA;  37530 MW;  B84585B44937B056 CRC64;
     MSLLITSLAW GALLDPEVSS ASKVALLDAV LEASTLLLRQ NGSVRKFLAL VAVLCLAEKT
     GSDNLPALIL GSISTAASLS LHLETALRKS CVSNDQAVQT KRAMWILYCI DKSYALRWQT
     FSLVGDGSLP TTNPPDTALP SEVATTLSLE WLRIRSQYSK ICSNILQLGV GAEGEPSENR
     SNRAVVLSAA LEEWYGSVEI SQMMLSLEHS DAVHMKLQTS YHYYEARFQL LSISLPDPRS
     SSPTGSQECR EVLRRSIREV ITGSNTITSE YLLQDCNHLF IQTLALSMLA LDILLESDQG
     CGKENRALLS IVAGFFARVD IILPQSSIFE EVSNLIEILT YR