AMT13_ALTAL
ID AMT13_ALTAL Reviewed; 118 AA.
AC C9K7C5;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Thioredoxin AMT13 {ECO:0000255|PIRNR:PIRNR000077};
DE AltName: Full=AM-toxin biosynthesis protein 13 {ECO:0000303|PubMed:17990954};
GN Name=AMT13 {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: Thioredoxin; part of the gene clusters that mediate the
CC biosynthesis of AM-toxins, host-selective toxins (HSTs) causing
CC Alternaria blotch on apple, a worldwide distributed disease (Probable).
CC AM-toxins are cyclic depsipeptides containing the 3 residues 2-hydroxy-
CC isovaleric acid (2-HIV), dehydroalanine, L-alanine which are common for
CC all 3 AM-toxins I to III. The fourth precursor is L-alpha-amino-
CC methoxyphenyl-valeric acid (L-Amv) for AM-toxin I, L-alpha-amino-
CC phenyl-valeric acid (L-Apv) for AM-toxin II, and L-alpha-amino-
CC hydroxyphenyl-valeric acid (L-Ahv) for AM-toxin III (Probable). AM-
CC toxins have two target sites for affecting susceptible apple cells;
CC they cause invagination of the plasma membrane and electrolyte loss and
CC chloroplast disorganization (PubMed:22846083). The non-ribosomal
CC peptide synthetase AMT1 contains 4 catalytic modules and is responsible
CC for activation of each residue in AM-toxin (PubMed:10875335). The aldo-
CC keto reductase AMT2 catalyzes the conversion of 2-keto-isovaleric acid
CC (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV), one of the precursor
CC residues incorporated by AMT1 during AM-toxin biosynthesis, by
CC reduction of its ketone to an alcohol (PubMed:15066029). The cytochrome
CC P450 monooxygenase AMT3 and the thioesterase AMT4 are also important
CC for AM-toxin production, but their exact function within the AM-toxin
CC biosynthesis are not known yet (PubMed:17990954). Up to 21 proteins
CC (including AMT1 to AMT4) are predicted to be involved in AM-toxin
CC biosynthesis since their expression ishighly up-regulated in AM-toxin-
CC producing cultures (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}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AB525198; BAI44749.1; -; Genomic_DNA.
DR EMBL; AB525199; BAI44776.1; -; Genomic_DNA.
DR AlphaFoldDB; C9K7C5; -.
DR SMR; C9K7C5; -.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Redox-active center; Virulence.
FT CHAIN 1..118
FT /note="Thioredoxin AMT13"
FT /id="PRO_0000444865"
FT DOMAIN 1..110
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 36..39
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 118 AA; 13103 MW; A13AC7958C42AF2C CRC64;
MSDNKAIQTL QNTKEFNEVI KVKGSLIIFD CFSTWCGPCK VIDPQILKLS QAYSDTYFYK
LNVDEVPDVA QKLDIRFVPT FLLFKDGEKV AEVVGAKPKA LEDAIRANLG CGATHSSN
