ACTS2_ALTAL
ID ACTS2_ALTAL Reviewed; 343 AA.
AC D7UPN2;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Trans-enoyl reductase ACTTS2 {ECO:0000303|PubMed:20055645};
DE EC=1.-.-.- {ECO:0000305|PubMed:20055645};
DE AltName: Full=ACT-toxin biosynthesis protein S2 {ECO:0000303|PubMed:20055645};
GN Name=ACTTS2 {ECO:0000303|PubMed:20055645};
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=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 [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=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 [4]
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 [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).
CC -!- FUNCTION: Trans-enoyl reductase; part of the gene clusters that mediate
CC the biosynthesis of the host-selective toxins (HSTs) ACT-toxins
CC responsible for brown spot of tangerine disease by the tangerine
CC pathotype which affects tangerines and mandarins (PubMed:19271978).
CC ACT-toxins consist of three moieties, 9,10-epoxy-8-hydroxy-9-methyl-
CC decatrienoic acid (EDA), valine and a polyketide (PubMed:22846083).
CC ACT-toxin I is toxic to both citrus and pear; toxin II the 5''-deoxy
CC derivative of ACT-toxin I, is highly toxic to pear and slightly toxic
CC to citrus (PubMed:22846083). On cellular level, ACT-toxins affect
CC plasma membrane of susceptible cells and cause a sudden increase in
CC loss of K(+) after a few minutes of toxin treatment (PubMed:22846083).
CC The acyl-CoA ligase ACTT1, the hydrolase ACTT2, the enoyl-CoA
CC hydratases ACTT3 and ACTT6, and the acyl-CoA synthetase ACTT5 are all
CC involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-
CC epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety
CC (PubMed:18944496, PubMed:18986255, PubMed:19271978). The exact role of
CC each enzyme, and of additional enzymes identified within the AF-toxin
CC clusters have 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:20055645}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC -!- DISRUPTION PHENOTYPE: Targeted gene disruption leasd to a reduction in
CC ACT-toxin production and pathogenicity, and transcriptional knockdown
CC of ACTTS2 using RNA silencing results in complete loss of ACT-toxin
CC production and pathogenicity (PubMed:20055645). Does not affect growth
CC rate, spore formation, and spore germination (PubMed:20055645).
CC {ECO:0000269|PubMed:20055645}.
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 zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB510353; BAJ09790.1; -; Genomic_DNA.
DR EMBL; AB516322; BAJ14523.1; -; Genomic_DNA.
DR AlphaFoldDB; D7UPN2; -.
DR SMR; D7UPN2; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..343
FT /note="Trans-enoyl reductase ACTTS2"
FT /id="PRO_0000444864"
FT BINDING 42..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 128..135
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 162..165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 185..188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 268..272
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 333..334
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 343 AA; 36508 MW; 1B0DD0986AB903CB CRC64;
MLTRRALVVQ SQGEVQVEEI PLPTLRDEYI TVKVKAVALN PGDWKMLYGP HATPGSILGC
DYSGVVEKVG RAVNALLTPG DRVAGFAFGG CPYNHDEGGF ASYVTAKGDI QAKLSDSISF
EDAATLGVGI TTVGQAMYQA LGLPLPPAII QEAASILVYG ASTATGTLAV QYAKLTGLKV
FATASPHNFD LLKKLGADEV FDYRDPECGA KIRTVTNGLL SLVFDTISEG SSPAIWAAAM
GAKGGKYTAL LPIKNFPRSD VKVTTILGYT ALGVKVSDHL PANQKDFEFS AKFWKLSQHL
LEKEKIKTHP VGVRQGGIDA IPQGLQDLKN GRVSGVKLVY KID
