AFT21_ALTAL
ID AFT21_ALTAL Reviewed; 262 AA.
AC B2DFU4;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Abhydrolase domain-containing protein AFT2-1 {ECO:0000303|PubMed:18986255};
DE EC=3.1.1.- {ECO:0000305|PubMed:18986255};
DE AltName: Full=AF-toxin biosynthesis protein 2-1 {ECO:0000303|PubMed:18986255};
GN Name=AFT2-1 {ECO:0000303|PubMed:18986255};
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=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 [2]
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 [3]
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 [4]
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 [5]
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 [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: Abhydrolase domain-containing protein; part of the gene
CC clusters that mediate the biosynthesis of the host-selective toxins
CC (HSTs) AF-toxins responsible for Alternaria black spot of strawberry
CC disease by the strawberry pathotype (PubMed:18986255). AF-toxin I and
CC III are valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-
CC hydroxy-isovaleric acid respectively, while AF II is an isoleucine
CC derivative of 2-hydroxy-valeric acid (PubMed:15066029, Ref.5,
CC PubMed:22846083). These derivatives are bound to a 9,10-epoxy-8-
CC hydroxy-9-methyl-decatrienoic acid (EDA) moiety (PubMed:15066029,
CC Ref.5, PubMed:22846083). On cellular level, AF-toxins affect plasma
CC membrane of susceptible cells and cause a sudden increase in loss of
CC K(+) after a few minutes of toxin treatment (PubMed:22846083). The
CC aldo-keto reductase AFTS1 catalyzes the conversion of 2-keto-isovaleric
CC acid (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV) by reduction of its
CC ketone to an alcohol (PubMed:15066029). The acyl-CoA ligase AFT1, the
CC hydrolase AFT2 and the enoyl-CoA hydratases AFT3 and AFT6, but also the
CC polyketide synthase AFT9, the acyl-CoA dehydrogenase AFT10, the
CC cytochrome P450 monooxygenase AFT11 and the oxidoreductase AFT12 are
CC all involved in the biosynthesis of the AK-, AF- and ACT-toxin common
CC EDA structural moiety (PubMed:12019223, Ref.5, PubMed:18986255). The
CC exact function of each enzyme, and of additional enzymes identified
CC within the AF-toxin clusters have still to be determined
CC (PubMed:12019223, Ref.5, PubMed:18986255).
CC {ECO:0000269|PubMed:12019223, ECO:0000269|PubMed:15066029,
CC ECO:0000269|PubMed:18986255, ECO:0000269|Ref.5,
CC ECO:0000303|PubMed:22846083}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:18986255}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O93801}.
CC Note=The peroxisomal location requires the C-terminal tripeptide
CC peroxisomal targeting signal. {ECO:0000250|UniProtKB:O93801}.
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 AB hydrolase superfamily. AKT2 hydrolase
CC family. {ECO:0000305}.
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DR EMBL; AB434468; BAG24496.1; -; Genomic_DNA.
DR EMBL; AB872925; BAO10619.1; -; Genomic_DNA.
DR AlphaFoldDB; B2DFU4; -.
DR SMR; B2DFU4; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase; Peroxisome; Virulence.
FT CHAIN 1..262
FT /note="Abhydrolase domain-containing protein AFT2-1"
FT /id="PRO_0000444824"
FT MOTIF 260..262
FT /note="Peroxisomal targeting signal type 1"
FT /evidence="ECO:0000250|UniProtKB:O93801"
SQ SEQUENCE 262 AA; 29372 MW; EC015108ED8A4E5D CRC64;
MQQPIVGVGH SMGGCQIATL SVTSRRMFST MILLDPAIGP LDMGLATLGL GQLTLRRRTQ
WPTREDAEKA LRTSFSTWDP QVLDLLIRHS IHSDKQSIEM EDGPVSLVTG RYQELVNYIK
PSFIRSGKVN GQELVHQTGP VDMYHMLGLV TCSALYLCGG ESTLSVPRAR DLWLSRTAKL
SYSKEPGETR KVDERVVPDT GHFLPMEEPK ECADIIADWI EKDECIAWNC CLGKRGKTWR
ELSNASKEMG AEAWMEYLQS KL
