ACTT3_ALTAL
ID ACTT3_ALTAL Reviewed; 296 AA.
AC Q589W8;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Enoyl-CoA hydratase ACTT3 {ECO:0000250|UniProtKB:Q9P4U9};
DE EC=4.2.1.17 {ECO:0000250|UniProtKB:Q9P4U9};
DE AltName: Full=ACT-toxin biosynthesis protein 3 {ECO:0000303|Ref.1};
GN Name=ACTT3 {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=SH20;
RA Masunaka A., Ishikura K., Asada K., Ohtsuki R., Tanaka A., Tsuge T.,
RA Peever T.L., Timmer L.W., Yamamoto M., Yamamoto H., Akimitsu K.;
RT "The pathway-specific regulatory protein ACTTR in the tangerine pathotype
RT of Alternaria alternata activates ACTT3 required for ACT-toxin
RT biosynthesis.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, AND PATHWAY.
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 [7]
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: Enoyl-CoA hydratase; 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:18944496,
CC PubMed:18986255). ACT-toxins consist of three moieties, 9,10-epoxy-8-
CC hydroxy-9-methyl-decatrienoic acid (EDA), valine and a polyketide
CC (PubMed:22846083). ACT-toxin I is toxic to both citrus and pear; toxin
CC II the 5''-deoxy derivative of ACT-toxin I, is highly toxic to pear and
CC slightly toxic to citrus (PubMed:22846083). On cellular level, ACT-
CC toxins affect plasma membrane of susceptible cells and cause a sudden
CC increase in loss of K(+) after a few minutes of toxin treatment
CC (PubMed:22846083). The acyl-CoA ligase ACTT1, the hydrolase ACTT2, the
CC enoyl-CoA hydratases ACTT3 and ACTT6, and the acyl-CoA synthetase ACTT5
CC are all involved in the biosynthesis of the AK-, AF- and ACT-toxin
CC common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural
CC moiety (PubMed:18944496, PubMed:18986255, PubMed:19271978). The exact
CC role of each enzyme, and of additional enzymes identified within the
CC AF-toxin clusters have still to be determined (PubMed:18944496,
CC PubMed:18986255, PubMed:19271978). On the other hand, ACTTS1 to ACTTS4
CC are specific to the tangerine pathotype (PubMed:22846083). The function
CC of ACTTS3 is to elongate the polyketide chain portion of ACT-toxin that
CC is unique to this toxin (PubMed:20192828). The enoyl-reductase ACTTS2
CC might complement the missing enoyl-reductase (ER) domain in ACTTS3 in
CC the synthesis of the polyketide portion of ACT-toxin (PubMed:20055645).
CC The roles of the nonribosomal peptide synthetases-related proteins
CC ACTTS1 and ACTTS4 have also still not been elucidated
CC (PubMed:22846083). {ECO:0000269|PubMed:18944496,
CC ECO:0000269|PubMed:18986255, ECO:0000269|PubMed:19271978,
CC ECO:0000269|PubMed:20055645, ECO:0000269|PubMed:20192828,
CC ECO:0000303|PubMed:22846083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:58856; EC=4.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q9P4U9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC ChEBI:CHEBI:137480; EC=4.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q9P4U9};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:18986255}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q9P4U9}.
CC Note=The peroxisomal location requires the C-terminal tripeptide
CC peroxisomal targeting signal. {ECO:0000250|UniProtKB:Q9P4U9}.
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 could not be accomplished due to the high
CC number of the copies identified in the genome, the high sequence
CC identity among these copies is likely an advantage for RNA silencing,
CC because it allows knockdown of all copies of this gene simultaneously
CC (PubMed:18986255). {ECO:0000269|PubMed:18986255}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AB176852; BAD93201.1; -; Genomic_DNA.
DR EMBL; AB176941; BAD93203.1; -; Genomic_DNA.
DR AlphaFoldDB; Q589W8; -.
DR SMR; Q589W8; -.
DR OrthoDB; 804458at2759; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
PE 3: Inferred from homology;
KW Lyase; Peroxisome; Virulence.
FT CHAIN 1..296
FT /note="Enoyl-CoA hydratase ACTT3"
FT /id="PRO_0000444833"
FT MOTIF 294..296
FT /note="Peroxisomal targeting signal type 1"
FT /evidence="ECO:0000250|UniProtKB:Q9P4U9"
SQ SEQUENCE 296 AA; 32200 MW; 726B868A3733DDE3 CRC64;
MLNRFSYSSN AWHNLRVDGP DADGIAVIVL ARSQSRNALT LPMLTDMVQL LSAMDADDSV
KCIVFTGEGQ FFCSGVDLTE GFGEIGKTRD THRDAGGKLA LAIHNCRKPT IAAINGTAVG
VGITMTLPMS IRIAAESAKI SFPFVRRGIV ADAASSFYLP RLIGYGRALH LFTTGALYPA
ESGLLHGLFS ETVNPASSTL PRALEVARDI AVNASQVGVY LTRDLIYRSL RSPEQAHLLE
SATLYTRYQS QDFEEGVKSF LEKRRPRFQD TMHEQSGEGV LERGDCVVSL ASKPKL
