AMT10_ALTAL
ID AMT10_ALTAL Reviewed; 900 AA.
AC C9K7C1;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Nonribosomal peptide synthetase AMT10 {ECO:0000250|UniProtKB:Q5AUZ6};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:Q5AUZ6};
DE AltName: Full=AM-toxin biosynthesis protein 10 {ECO:0000303|PubMed:17990954};
GN Name=AMT10 {ECO:0000303|PubMed:17990954};
GN Synonyms=AMT10-2 {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: Nonribosomal peptide synthetase; part of the gene clusters
CC that mediate the biosynthesis of AM-toxins, host-selective toxins
CC (HSTs) causing Alternaria blotch on apple, a worldwide distributed
CC disease (Probable). AM-toxins are cyclic depsipeptides containing the 3
CC residues 2-hydroxy-isovaleric acid (2-HIV), dehydroalanine, L-alanine
CC which are common for all 3 AM-toxins I to III. The fourth precursor is
CC L-alpha-amino-methoxyphenyl-valeric acid (L-Amv) for AM-toxin I, L-
CC alpha-amino-phenyl-valeric acid (L-Apv) for AM-toxin II, and L-alpha-
CC amino-hydroxyphenyl-valeric acid (L-Ahv) for AM-toxin III (Probable).
CC AM-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 -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Occasionally,
CC epimerase (E) domains (responsible for L- to D-amino acid conversion)
CC are present within the NRP synthetase (By similarity). AMT10 is
CC composed of only one module and misses a condensation (C) domain
CC (Probable). {ECO:0000250|UniProtKB:Q4WAZ9, ECO:0000305}.
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 NRP synthetase family. {ECO:0000305}.
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DR EMBL; AB525198; BAI44745.1; -; Genomic_DNA.
DR EMBL; AB525199; BAI44768.1; -; Genomic_DNA.
DR EMBL; AB525200; BAI44810.1; -; Genomic_DNA.
DR AlphaFoldDB; C9K7C1; -.
DR SMR; C9K7C1; -.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Ligase; Phosphopantetheine; Phosphoprotein; Virulence.
FT CHAIN 1..900
FT /note="Nonribosomal peptide synthetase AMT10"
FT /id="PRO_0000444813"
FT DOMAIN 824..900
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 284..686
FT /note="Adenylation"
FT /evidence="ECO:0000255"
FT MOD_RES 861
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 900 AA; 98347 MW; E4B62770C965EA2D CRC64;
MYCDKGASSL ANGLLPNVSG DITAKDNILD ALDSSAEEHF WGRYIDGFEG QIFPQIPVSV
HEAHLTGRAR YEIILGNSMV TTLYTVSSII RTGWALLVSQ YTESQDVVIV SSLELPSQAM
GGTILFPIRF RIRQDGRTEE LLQSAKKHAD KVLSSQKHDF PHTKDFVDPF SNSILLICTE
SQPSHSLEEL LTELSASKKC ALVLRCELLE DKISISAMFD PQVVRPRQTR RILDQLGHIL
KQISGSDMLV GDLDFLSPED RQEIGRWNSR SALSDECIHA LISKQAQQNP AAMAVNAHDG
NFTYGELESY ATRLAAHLIH IGVKPGNFVP TLFEKSKWTQ VGILAILKAG AAFVMLDPSH
PPARNQLICR KANACFALAS APCEPVLSMA VPHVITLSHS FMEELGRLQP PHEQKSPCLD
PRAVAYLLFT SGSTGQPKGA ILEHRSFAAA SRGVVAMTHM SSTTRTLQHS SYSFGAAIVE
IIATLVAGGC VVVLSDTERL SNVAASMVAY SVNWAFMTPS FARTVNPADV PCLRVLATGG
EGVTSDIVET WASFVSLYTV YGSAEQSSIA AMAGPLATHQ RGNSANVGSP FAGCYAWIVQ
PDRPEKLAPV GCVGELVLEG ALVARGYIDE VESTAAAFPK GFSWRCLFPL HQEGSTRFYR
TGDLVRYAVD GTLEFVARRN GYIKLRGQRI ELGEIESQLK AVARQPYEFC VEVVVPKGET
ADKAVLVAFV ALGSAYTDNE ICESAISSPE QFDQGILVDV LGHVEERLAE TLPAFMIPRF
FFPLQHFPVT SSGKIARKIL REQAAQMSVL QLAELSLGSV EKKELQSDME RYLRSVWVQL
LGVPEDFIGA NDSFFRVGGD SLKAIKLFQR LRRDGYNLNV TSIVAAPTLS QMARNCSLLD
