AM122_ALTAL
ID AM122_ALTAL Reviewed; 623 AA.
AC C9K7F3;
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 12-2 {ECO:0000303|Ref.1};
GN Name=AMT12-2 {ECO:0000303|Ref.1};
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].
RC STRAIN=NBRC 8984;
RA Harimoto Y., Kodama M., Yamamoto M., Otani H., Tsuge T.;
RT "A Zn(II)2Cys6 transcription regulator encoded by the AMT gene cluster
RT negatively controls AM-toxin production in the apple pathotype of
RT Alternaria alternata.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION.
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 [5]
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 (By similarity). AM-toxins are
CC cyclic depsipeptides containing the 3 residues 2-hydroxy-isovaleric
CC acid (2-HIV), dehydroalanine, L-alanine which are common for all 3 AM-
CC toxins I to III. The fourth precursor is L-alpha-amino-methoxyphenyl-
CC valeric acid (L-Amv) for AM-toxin I, L-alpha-amino-phenyl-valeric acid
CC (L-Apv) for AM-toxin II, and L-alpha-amino-hydroxyphenyl-valeric acid
CC (L-Ahv) for AM-toxin III (Probable). AM-toxins have two target sites
CC for 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:0000250|UniProtKB:C9K7C4,
CC ECO:0000269|PubMed:10875335, ECO:0000269|PubMed:15066029,
CC ECO:0000269|PubMed:17990954, ECO:0000303|PubMed:22846083,
CC ECO:0000305|PubMed:10875335}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:C9K7C4}.
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; AB525199; BAI44777.1; -; Genomic_DNA.
DR AlphaFoldDB; C9K7F3; -.
PE 2: Evidence at transcript level;
KW Virulence.
FT CHAIN 1..623
FT /note="AM-toxin biosynthesis protein 12-2"
FT /id="PRO_0000444847"
FT REGION 110..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 69456 MW; 4DE756F436A6497C CRC64;
MSKARSQDEV GWKRNESLCE YSMHRSRRPI QEKSIQSRAE HNFTLTRAYA INGSMTPDSS
NLHHSSQVAV GRDAEGSANT LNTPFSEACF SQLISDGARS YLDFDFPDET IPGTSQAKNT
EPDHQASGLQ NQMSCDSLRN NTIMLDWLDL DYDGNLRQYS TAQLYGLLGA DAHNGSAKCT
LSLLPERMVA DKAEAKLLLN HKMYGLTALC KNADRGSRRQ QAVWEKVEVL LSSKHQTCVS
DLLRKVDSSG EHQSLDLTSL PIEKLVQRAF RELGGLNLFI KEQDVTRIQE RFLDPEKLPV
DVSDMSLLIT SLAWGALLDP EKLQRCYFAR MVAFLCLAEK TGSDNLPALI LGSISTAASL
SLHLETALRK SCVSNDQAVQ TKRAMWILYC IDKSYALRWQ TFSLVGDGSL PTTNPPDTAL
PSEVATTLSL EWLRIRSQYS KICSNILQLG VGAEGEPSEN RSNRAVVLSA ALEEWYGSVE
ISQMMLSLEH SDAVHMKLQT SYHYYEARFQ LLSISLPDPR SSSPTGSQEC REVLRRSIRE
VITGSNTITS EYLLQDCNHL FIQTLALSML ALDILLESDQ GCGKENRALL SIVAGFFARV
DIILPQSSIF EEVSNLIEIL TYR