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AKT31_ALTAL
ID   AKT31_ALTAL             Reviewed;         296 AA.
AC   Q9P4U9;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Enoyl-CoA hydratase AKT3-1 {ECO:0000303|PubMed:10975654};
DE            EC=4.2.1.17 {ECO:0000305|PubMed:10975654};
DE   AltName: Full=AF-toxin biosynthesis protein 3-1 {ECO:0000303|PubMed:10975654};
GN   Name=AKT3-1 {ECO:0000303|PubMed:10975654};
GN   Synonyms=AKT3-3 {ECO:0000303|PubMed:24611558};
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=15A;
RX   PubMed=10975654; DOI=10.1094/mpmi.2000.13.9.975;
RA   Tanaka A., Tsuge T.;
RT   "Structural and functional complexity of the genomic region controlling AK-
RT   toxin biosynthesis and pathogenicity in the Japanese pear pathotype of
RT   Alternaria alternata.";
RL   Mol. Plant Microbe Interact. 13:975-986(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=15A;
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=15A;
RX   PubMed=10432635; DOI=10.1094/mpmi.1999.12.8.691;
RA   Tanaka A., Shiotani H., Yamamoto M., Tsuge T.;
RT   "Insertional mutagenesis and cloning of the genes required for biosynthesis
RT   of the host-specific AK-toxin in the Japanese pear pathotype of Alternaria
RT   alternata.";
RL   Mol. Plant Microbe Interact. 12:691-702(1999).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20348386; DOI=10.1128/ec.00369-09;
RA   Imazaki A., Tanaka A., Harimoto Y., Yamamoto M., Akimitsu K., Park P.,
RA   Tsuge T.;
RT   "Contribution of peroxisomes to secondary metabolism and pathogenicity in
RT   the fungal plant pathogen Alternaria alternata.";
RL   Eukaryot. Cell 9:682-694(2010).
RN   [5]
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) AK-toxins
CC       responsible for Japanese pear black spot disease by the Japanese pear
CC       pathotype (PubMed:10975654, PubMed:10432635, PubMed:20348386). AK-
CC       toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid
CC       (EDA) (PubMed:22846083). On cellular level, AK-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       acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3
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:10432635, PubMed:10975654, PubMed:22846083). Part of the
CC       EDA biosynthesis occurs in the peroxisome since these 3 enzymes are
CC       localized in peroxisomes (PubMed:20348386). The exact roles of the 3
CC       enzymes, as well as of additional AK-toxin clusters enzymes, including
CC       AKT4, AKT6 and AKTS1, have still to be elucidated (PubMed:10432635,
CC       PubMed:10975654, PubMed:22846083). The Cytochrome P450 monooxygenase
CC       AKT7 on the other side functions to limit production of EDA and AK-
CC       toxin, probably via the catalysis of a side reaction of EDA or its
CC       precursor (PubMed:24611558). {ECO:0000269|PubMed:10432635,
CC       ECO:0000269|PubMed:10975654, ECO:0000269|PubMed:20348386,
CC       ECO:0000269|PubMed:24611558, 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:0000305|PubMed:10975654};
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:0000305|PubMed:10975654};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:10975654}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:20348386}.
CC       Note=The peroxisomal location requires the C-terminal tripeptide
CC       peroxisomal targeting signal. {ECO:0000269|PubMed:20348386}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of AF-toxins and their
CC       precuror 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid; and impairs
CC       the pathogenicity. {ECO:0000269|PubMed:10975654}.
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:10975654). The CDCs are not essential for saprophytic growth
CC       but controls host-selective pathogenicity (PubMed:10975654).
CC       {ECO:0000269|PubMed:10975654}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AB035492; BAB07811.1; -; Genomic_DNA.
DR   EMBL; AB872924; BAO10616.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P4U9; -.
DR   SMR; Q9P4U9; -.
DR   PHI-base; PHI:2832; -.
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 AKT3-1"
FT                   /id="PRO_0000444831"
FT   MOTIF           294..296
FT                   /note="Peroxisomal targeting signal type 1"
FT                   /evidence="ECO:0000269|PubMed:20348386"
SQ   SEQUENCE   296 AA;  32127 MW;  E8E637D475900816 CRC64;
     MLNRFSYSSN AWHNLRVDGP DADGIAVIVL ARSQSRNALT LPMLTDMVQL LSAMDADDSV
     KCIVFTGEGP FFCSGVDLTE GFGEIGKTRD THRDAGGKLA LAIHNCRKPT IAAINGTAVG
     VGITMTLPMS IRIAAKTAKI SFPFVRRGIV ADAASSFYLP RLVGYGRALH LFTTGALYPA
     ESGLLHGLFS ETVNPASSTL PRALEVARDI AVNASQVGVY LTRDLVYRSP RSPEQAHLLE
     SAALYTRYQS RDFEEGVKSF LEKRKPRFQD TMREQSSEGV LERGDCVVGL ASKPKL
 
 
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