ACT23_ALTAL
ID ACT23_ALTAL Reviewed; 177 AA.
AC C9K1N0;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Abhydrolase domain-containing protein ACTT2-3 {ECO:0000303|PubMed:18986255};
DE EC=3.1.1.- {ECO:0000305|PubMed:18986255};
DE AltName: Full=ACT-toxin biosynthesis protein 2-3 {ECO:0000303|PubMed:18986255};
DE Flags: Fragment;
GN Name=ACTT2-3 {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, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=BC3-5-1-OS2A;
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 FUNCTION.
RX PubMed=18944496; DOI=10.1094/phyto.2000.90.7.762;
RA Masunaka A., Tanaka A., Tsuge T., Peever T.L., Timmer L.W., Yamamoto M.,
RA Yamamoto H., Akimitsu K.;
RT "Distribution and characterization of AKT homologs in the tangerine
RT pathotype of Alternaria alternata.";
RL Phytopathology 90:762-768(2000).
RN [3]
RP FUNCTION.
RC STRAIN=SH20;
RX PubMed=19271978; DOI=10.1094/phyto-99-4-0369;
RA Miyamoto M., Ishii Y., Honda A., Masunaka A., Tsuge T., Yamamoto M.,
RA Ohtani K., Fukumoto T., Gomi K., Peever T.L., Akimitsu K.;
RT "Function of genes encoding acyl-CoA synthetase and enoyl-CoA hydratase for
RT host-selective act-toxin biosynthesis in the tangerine pathotype of
RT Alternaria alternata.";
RL Phytopathology 99:369-377(2009).
RN [4]
RP FUNCTION.
RC STRAIN=SH20;
RX PubMed=20055645; DOI=10.1094/phyto-100-2-0120;
RA Ajiro N., Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K.,
RA Fukumoto T., Gomi K., Peever T.L., Izumi Y., Tada Y., Akimitsu K.;
RT "Role of the host-selective ACT-toxin synthesis gene ACTTS2 encoding an
RT enoyl-reductase in pathogenicity of the tangerine pathotype of Alternaria
RT alternata.";
RL Phytopathology 100:120-126(2010).
RN [5]
RP FUNCTION.
RC STRAIN=SH20;
RX PubMed=20192828; DOI=10.1094/mpmi-23-4-0406;
RA Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K., Fukumoto T.,
RA Gomi K., Peever T.L., Tada Y., Ichimura K., Akimitsu K.;
RT "ACTTS3 encoding a polyketide synthase is essential for the biosynthesis of
RT ACT-toxin and pathogenicity in the tangerine pathotype of Alternaria
RT alternata.";
RL Mol. Plant Microbe Interact. 23:406-414(2010).
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).
RN [7]
RP INDUCTION.
RX PubMed=29616013; DOI=10.3389/fmicb.2018.00508;
RA Wang M., Yang X., Ruan R., Fu H., Li H.;
RT "Csn5 is required for the conidiogenesis and pathogenesis of the Alternaria
RT alternata tangerine pathotype.";
RL Front. Microbiol. 9:508-508(2018).
CC -!- FUNCTION: Abhydrolase domain-containing protein; part of the gene
CC clusters that mediate the biosynthesis of the host-selective toxins
CC (HSTs) ACT-toxins responsible for brown spot of tangerine disease by
CC the tangerine pathotype which affects tangerines and mandarins
CC (PubMed:18944496, PubMed:18986255). ACT-toxins consist of three
CC moieties, 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA), valine
CC and a polyketide (PubMed:22846083). ACT-toxin I is toxic to both citrus
CC and pear; toxin II the 5''-deoxy derivative of ACT-toxin I, is highly
CC toxic to pear and slightly toxic to citrus (PubMed:22846083). On
CC cellular level, ACT-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 acyl-CoA ligase ACTT1, the
CC hydrolase ACTT2, the enoyl-CoA hydratases ACTT3 and ACTT6, and the
CC acyl-CoA synthetase ACTT5 are all involved in the biosynthesis of the
CC AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-
CC decatrienoic acid (EDA) structural moiety (PubMed:18944496,
CC PubMed:18986255, PubMed:19271978). The exact role of each enzyme, and
CC of additional enzymes identified within the AF-toxin clusters have
CC still to be determined (PubMed:18944496, PubMed:18986255,
CC PubMed:19271978). On the other hand, ACTTS1 to ACTTS4 are specific to
CC the tangerine pathotype (PubMed:22846083). The function of ACTTS3 is to
CC elongate the polyketide chain portion of ACT-toxin that is unique to
CC this toxin (PubMed:20192828). The enoyl-reductase ACTTS2 might
CC complement the missing enoyl-reductase (ER) domain in ACTTS3 in the
CC synthesis of the polyketide portion of ACT-toxin (PubMed:20055645). The
CC roles of the nonribosomal peptide synthetases-related proteins ACTTS1
CC and ACTTS4 have also still not been elucidated (PubMed:22846083).
CC {ECO:0000269|PubMed:18944496, ECO:0000269|PubMed:18986255,
CC ECO:0000269|PubMed:19271978, ECO:0000269|PubMed:20055645,
CC ECO:0000269|PubMed:20192828, ECO:0000303|PubMed:22846083}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|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 -!- INDUCTION: Expression is positively regulated by CSN5 during infection.
CC {ECO:0000269|PubMed:29616013}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of ACT-toxin and impairs
CC the formation of lesions on leaves sprayed with conidia
CC (PubMed:18986255). Does not affect growth rate of cultures,
CC sporulation, and spore germination (PubMed:18986255).
CC {ECO:0000269|PubMed:18986255}.
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:18986255). The CDCs are not essential for saprophytic growth
CC but controls host-selective pathogenicity (PubMed:18986255). Although
CC conventional disruption of ACTT2 could not be accomplished due to the
CC high number of the copies identified in the genome, the high sequence
CC identity among these copies of ACTT2 is likely an advantage for RNA
CC silencing, because it allows knockdown of all copies of this gene
CC simultaneously (PubMed:18986255). {ECO:0000269|PubMed:18986255}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AKT2 hydrolase
CC family. {ECO:0000305}.
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DR EMBL; AB432917; BAI44324.1; -; Genomic_DNA.
DR AlphaFoldDB; C9K1N0; -.
DR SMR; C9K1N0; -.
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 2: Evidence at transcript level;
KW Hydrolase; Peroxisome; Virulence.
FT CHAIN 1..>177
FT /note="Abhydrolase domain-containing protein ACTT2-3"
FT /id="PRO_0000444829"
FT NON_TER 177
FT /evidence="ECO:0000305"
SQ SEQUENCE 177 AA; 19460 MW; 593E3483939C699C CRC64;
MQQPIVGVGH SMGGCQIATL SVTSRRIFST MILLDPAIGP PEMGLATLGL GQLTLRRRTQ
WLTREDAEKA LRTSFSTWDP QVLDLLIKHS IHSDKQSVEM EDGPVSLVTG RYQELVNYIK
PSFIRSGKVV GQELVHQTGP VDMYHMLGLV TCSTLYLCGG ESTLSTPRAR ESYGLAE
