AMT2_ALTAL
ID AMT2_ALTAL Reviewed; 367 AA.
AC Q75ZG2;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Aldo-keto reductase AMT2 {ECO:0000303|PubMed:15066029};
DE EC=1.1.1.- {ECO:0000305|PubMed:15066029};
DE AltName: Full=AM-toxin biosynthesis protein 2 {ECO:0000303|PubMed:15066029};
GN Name=AMT2 {ECO:0000303|PubMed:15066029};
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], FUNCTION, AND PATHWAY.
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
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 [3]
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 [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: Aldo-keto reductase; part of the gene clusters that mediate
CC the biosynthesis of AM-toxins, host-selective toxins (HSTs) causing
CC Alternaria blotch on apple, a worldwide distributed disease
CC (PubMed:10875335, PubMed:17990954). AM-toxins are cyclic depsipeptides
CC containing the 3 residues 2-hydroxy-isovaleric acid (2-HIV),
CC dehydroalanine, L-alanine which are common for all 3 AM-toxins I to
CC III. The fourth precursor is L-alpha-amino-methoxyphenyl-valeric acid
CC (L-Amv) for AM-toxin I, L-alpha-amino-phenyl-valeric acid (L-Apv) for
CC AM-toxin II, and L-alpha-amino-hydroxyphenyl-valeric acid (L-Ahv) for
CC AM-toxin III (Probable). AM-toxins have two target sites for affecting
CC susceptible apple cells; they cause invagination of the plasma membrane
CC and electrolyte loss and chloroplast disorganization (PubMed:22846083).
CC The non-ribosomal peptide synthetase AMT1 contains 4 catalytic modules
CC and is responsible for activation of each residue in AM-toxin
CC (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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:15066029}.
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 aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AB525198; BAC84994.1; -; Genomic_DNA.
DR EMBL; AB525199; BAI44761.1; -; Genomic_DNA.
DR EMBL; AB525200; BAI44803.1; -; Genomic_DNA.
DR AlphaFoldDB; Q75ZG2; -.
DR SMR; Q75ZG2; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 2: Evidence at transcript level;
KW NADP; Oxidoreductase; Virulence.
FT CHAIN 1..367
FT /note="Aldo-keto reductase AMT2"
FT /id="PRO_0000444816"
FT REGION 346..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 81
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 203..204
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 229
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 258..268
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 330..338
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
SQ SEQUENCE 367 AA; 41496 MW; 572D7C01BA9DCB20 CRC64;
MLNYKKWTQP PNSLIKSIKA SRAAYRRLGN SGLLVSNPIL GGMHIGDPRW YDWVLDEKDS
IALLKAAYDR GINTWDTANI YSNGESERIM GRALRSHNIP RSKVVIMTKC FRAVTDPDVD
GDIGSSTAFF PDLTRQSKDY VNHCGLSRAS VFQQVEASLR RLNTDYIDVL HIHRFDHHVP
PEETMKALHD LVQMNKVRYL GASSMWAHEF AILQHTAEKN NWTKFVSMQN HYNLLYREEE
REMIKYCNLT GVGLIPWGPL AAGKLARPPD GKASTFRAIN GGAYKDHNPA ESEQIARRVH
QIAVSRGVPM SHVALAWLNK RVVSPVIGLS SVERMDEVLD ARALELSDEE ESRLEDPYKA
QPPQGHS
