AMT9_ALTAL
ID AMT9_ALTAL Reviewed; 425 AA.
AC C9K7C0;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=O-methyltransferase AMT9 {ECO:0000250|UniProtKB:D7PI16};
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
DE AltName: Full=AM-toxin biosynthesis protein 9 {ECO:0000303|PubMed:17990954};
GN Name=AMT9 {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: O-methyltransferase; 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 (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 class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; AB525198; BAI44744.1; -; Genomic_DNA.
DR EMBL; AB525199; BAI44767.1; -; Genomic_DNA.
DR EMBL; AB525200; BAI44809.1; -; Genomic_DNA.
DR AlphaFoldDB; C9K7C0; -.
DR SMR; C9K7C0; -.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase; Virulence.
FT CHAIN 1..425
FT /note="O-methyltransferase AMT9"
FT /id="PRO_0000444858"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 257..258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 306..307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 322
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 323
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 425 AA; 47469 MW; 7BFE8834C5E37BF4 CRC64;
MHPASESSHI TRLAESIVAN TAIVNAYLCE QNLPLPRFDD INAAVRPCTA DDASAESARR
AVVTASQELR DLLSGPSAPL MVDWTAHSCL RTIVHFRLAE AVSLVPANDI GTSFANIAAQ
TSLSETHVTR ILRHAMTRHI FREPAPGFVA HTAASALLSR DSVTRDVVGL ITDEMWPAGL
KVPEALARWP NSQEPEETGF SMANAQGSEE QKKSMWSVYE EDAERARRFG VCMSVENSAM
PFPLEELEWQ GLVVDIGGGV GFNVFNLAEK HQNARFIVED LSKTVQQGRL LLPKQLKDRV
DFVEHDFFSP QPVKDADIYF FRRIFHDWSD KHAVEIIRSL IPALKPGARV RVNELLVPKP
GELPREIEKM ARNSDFAMLA LLNGKERNNE EWQALFRAAS DKFRFGFCKT TPPGLMAVIE
FVWEP
