AF151_ALTAL
ID AF151_ALTAL Reviewed; 517 AA.
AC V5XYQ7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Acyltransferase AFT15-1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305};
DE AltName: Full=AF-toxin biosynthesis protein 15-1 {ECO:0000305};
GN Name=AFT15-1;
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=NAF8;
RX PubMed=24611558; DOI=10.1111/nph.12754;
RA Takaoka S., Kurata M., Harimoto Y., Hatta R., Yamamoto M., Akimitsu K.,
RA Tsuge T.;
RT "Complex regulation of secondary metabolism controlling pathogenicity in
RT the phytopathogenic fungus Alternaria alternata.";
RL New Phytol. 202:1297-1309(2014).
RN [2]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=12019223; DOI=10.1093/genetics/161.1.59;
RA Hatta R., Ito K., Hosaki Y., Tanaka T., Tanaka A., Yamamoto M.,
RA Akimitsu K., Tsuge T.;
RT "A conditionally dispensable chromosome controls host-specific
RT pathogenicity in the fungal plant pathogen Alternaria alternata.";
RL Genetics 161:59-70(2002).
RN [3]
RP FUNCTION.
RC STRAIN=NAF8;
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=NAF8;
RX DOI=10.1007/s10327-004-0170-3;
RA Ruswandi S., Kitani K., Akimitsu K., Tsuge T., Shiraishi T., Yamamoto M.;
RT "Structural analysis of cosmid clone pcAFT-2 carrying AFT10-1 encoding an
RT acyl-CoA dehydrogenase involved in AF-toxin production in the strawberry
RT pathotype of Alternaria alternata.";
RL J. Gen. Plant Pathol. 71:107-116(2005).
RN [5]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=18986255; DOI=10.1094/mpmi-21-12-1591;
RA Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K., Fukumoto T.,
RA Gomi K., Peever T.L., Akimitsu K.;
RT "Functional analysis of a multicopy host-selective ACT-toxin biosynthesis
RT gene in the tangerine pathotype of Alternaria alternata using RNA
RT silencing.";
RL Mol. Plant Microbe Interact. 21:1591-1599(2008).
RN [6]
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: Acyltransferase; part of the gene clusters that mediate the
CC biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible
CC for Alternaria black spot of strawberry disease by the strawberry
CC pathotype (Probable). AF-toxin I and III are valine derivatives of 2,3-
CC dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively,
CC while AF II is an isoleucine derivative of 2-hydroxy-valeric acid
CC (PubMed:15066029, Ref.4, PubMed:22846083). These derivatives are bound
CC to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) moiety
CC (PubMed:15066029, Ref.4, PubMed:22846083). On cellular level, AF-toxins
CC affect plasma membrane of susceptible cells and cause a sudden increase
CC in loss of K(+) after a few minutes of toxin treatment
CC (PubMed:22846083). The aldo-keto reductase AFTS1 catalyzes the
CC conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric
CC acid (2-HIV) by reduction of its ketone to an alcohol
CC (PubMed:15066029). The acyl-CoA ligase AFT1, the hydrolase AFT2 and the
CC enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide synthase
CC AFT9, the acyl-CoA dehydrogenase AFT10, the cytochrome P450
CC monooxygenase AFT11 and the oxidoreductase AFT12 are all involved in
CC the biosynthesis of the AK-, AF- and ACT-toxin common EDA structural
CC moiety (PubMed:12019223, Ref.4, PubMed:18986255). The exact function of
CC each enzyme, and of additional enzymes identified within the AF-toxin
CC clusters have still to be determined (PubMed:12019223, Ref.4,
CC PubMed:18986255). {ECO:0000269|PubMed:12019223,
CC ECO:0000269|PubMed:15066029, ECO:0000269|PubMed:18986255,
CC ECO:0000269|Ref.4, ECO:0000303|PubMed:22846083,
CC ECO:0000305|PubMed:24611558}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {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:12019223). The CDCs are not essential for saprophytic growth
CC but controls host-selective pathogenicity (PubMed:12019223).
CC {ECO:0000269|PubMed:12019223}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AB872925; BAO10620.1; -; Genomic_DNA.
DR AlphaFoldDB; V5XYQ7; -.
DR SMR; V5XYQ7; -.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 3: Inferred from homology;
KW Transferase; Virulence.
FT CHAIN 1..517
FT /note="Acyltransferase AFT15-1"
FT /id="PRO_0000444863"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
SQ SEQUENCE 517 AA; 57074 MW; EB3F7785FD69086E CRC64;
MKVTITSIDQ VLPSVEITAP KSLALSHIDE WHSRGRSSLV WLYPKPKKPT QSLQLLDHLR
SSLSQALNKF PQYAGKLSHS LQTGTSQKSK TRLCLTWGTG NDPGVHYITA RASSPIDALL
PPLGTSTGFT NGSGSYAWDR SGRSCIGLWP AVPLNKVYET CIQITTFECG GFSLSITMNH
AVADATSVIL FARHWSKTHE LMVKVQTPSL SIAEPCFAPH LIDQYSTLEL QDEGDNGKLL
NKAHALPTLR NDLYESGARS LPDRLELSET YSVGDDIAVG DWERSGPMRS YMLHFSKEDI
NKIWESAKKE AGQDVSRQAA IVSYIWLAII RAREWDKHGV CEPIKLFITF DVRRRLGLPD
TLLGSPVLVT HVKFNGNDAI SKSHGLLANR IWKTLSTYDV ESVCAALYDI TSSRPLISPA
IWLGGRSTLF SSLCHADMYD VTFHETGPLL AAPAFAGMGG MIGLIKSKSA VPSRLPETYE
DGIDMFFELD TESSIKLFSD PALSIFDGRA LLQEFRQ
