AFT8_ALTAL
ID AFT8_ALTAL Reviewed; 402 AA.
AC V5XKK6;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Putative epoxide hydrolase AFT8 {ECO:0000250|UniProtKB:M2WIS5};
DE EC=3.-.-.- {ECO:0000250|UniProtKB:M2WIS5};
DE AltName: Full=AF-toxin biosynthesis protein 8 {ECO:0000303|Ref.1};
GN Name=AFT8 {ECO:0000303|Ref.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;
RA Kondou H., Hara A., Mase C., Harimoto Y., Tsuge T.;
RT "The gene cluster involved in AF-toxin biosynthesis of Alternaria
RT alternata.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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: Putative epoxide hydrolase; part of the gene clusters that
CC mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins
CC responsible for Alternaria black spot of strawberry disease by the
CC strawberry pathotype (Probable). AF-toxin I and III are valine
CC derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric
CC acid respectively, while AF II is an isoleucine derivative of 2-
CC hydroxy-valeric acid (PubMed:15066029, Ref.4, PubMed:22846083). These
CC derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic
CC acid (EDA) moiety (PubMed:15066029, Ref.4, PubMed:22846083). On
CC cellular level, AF-toxins affect plasma membrane of susceptible cells
CC and cause a sudden increase in loss of K(+) after a few minutes of
CC toxin treatment (PubMed:22846083). The aldo-keto reductase AFTS1
CC catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-
CC hydroxy-isovaleric acid (2-HIV) by reduction of its ketone to an
CC alcohol (PubMed:15066029). The acyl-CoA ligase AFT1, the hydrolase AFT2
CC and the enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide
CC synthase 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, ECO:0000305|Ref.1}.
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 peptidase S33 family. {ECO:0000305}.
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DR EMBL; AB873047; BAO05507.1; -; Genomic_DNA.
DR AlphaFoldDB; V5XKK6; -.
DR SMR; V5XKK6; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR010497; Epoxide_hydro_N.
DR Pfam; PF06441; EHN; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase; Virulence.
FT CHAIN 1..402
FT /note="Putative epoxide hydrolase AFT8"
FT /id="PRO_0000444844"
SQ SEQUENCE 402 AA; 44371 MW; F71C6EBD956CA692 CRC64;
MASYKNIPST AKGSPISFDF SFPQPKLDHL RQVLELHPLG REAPSKTLRG SSKPQWFGNA
KEIMRRFDWA AEEELLKAFP HYVVGVEDTI GGQMLQVHFV ALFSTSPDAI PVLLIHSWFS
SYVEYLCLLS VFTERFPQAC DLPFHVIVPS LPGYDFSSPL SRETNNAQIN EDNARVLNQL
MVNLGFGAGS GGIGGYVVHG GVSSLRMCYT LAKEYKDCRA LHANLDGAYR HTLTSSGGDE
FEAVKSVLAE LHPPEDWDSH ERDMIRLAIS TSPVSLLALI GSQFFGEQEQ GAALRMVALI
VAHHWMTDTY PDASQESYCI KDMSAEDLSH VLKHTGLEPN KPVGISFFSH GQGSASDIRP
IVDGSSWSSR HEGNPFVAVL DQPNQTVGDL LGFVRQVQKQ HS
