AKT32_ALTAL
ID AKT32_ALTAL Reviewed; 296 AA.
AC Q9P4U7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Enoyl-CoA hydratase AKT3-2 {ECO:0000303|PubMed:10975654};
DE EC=4.2.1.17 {ECO:0000305|PubMed:10975654};
DE AltName: Full=AK-toxin biosynthesis protein 3-2 {ECO:0000303|PubMed:10975654};
GN Name=AKT3-2 {ECO:0000303|PubMed:10975654};
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=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 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 [3]
RP FUNCTION.
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 [4]
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 [5]
RP 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).
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). AK-toxins are esters of 9,10-epoxy 8-
CC hydroxy 9-methyldecatrienoic acid (EDA) (PubMed:22846083). On cellular
CC level, AK-toxins affect plasma membrane of susceptible cells and cause
CC a sudden increase in loss of K(+) after a few minutes of toxin
CC treatment (PubMed:22846083). The acyl-CoA ligase AKT1, the hydrolase
CC AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis
CC of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-
CC decatrienoic acid (EDA) structural moiety (PubMed:10432635,
CC PubMed:10975654, PubMed:22846083). Part of the EDA biosynthesis occurs
CC in the peroxisome since these 3 enzymes are localized in peroxisomes
CC (PubMed:20348386). The exact roles of the 3 enzymes, as well as of
CC additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1,
CC have still to be elucidated (PubMed:10432635, PubMed:10975654,
CC PubMed:22846083). The Cytochrome P450 monooxygenase AKT7 on the other
CC side functions to limit production of EDA and AK-toxin, probably via
CC the catalysis of a side reaction of EDA or its precursor
CC (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:0000305|PubMed:10975654}.
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: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; AB035494; BAB07813.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P4U7; -.
DR SMR; Q9P4U7; -.
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 AKT3-2"
FT /id="PRO_0000444832"
FT MOTIF 294..296
FT /note="Peroxisomal targeting signal type 1"
FT /evidence="ECO:0000250|UniProtKB:Q9P4U9"
SQ SEQUENCE 296 AA; 32114 MW; 491B6CAD398221A1 CRC64;
MLNRFSYSSN AWHNLRVDGP DADGIAVIVL ARSQSRNALT LPMLTDMIQL LSAMDADDSV
KCIVFTGEGQ FFCSGVDLTE GFGEIGKTRD THRDAGGKLA LAIHNCCKPT IAAINGTAVG
VGITMTLPMS IRIAAKTAKI SFPFVRREIV ADAASSFYLP RLIGYGRALH LFTTGALYSA
ESGLLHGLFS ETVNSASSTL PRALEVARDI AINTSQVGGC LTRDLIYRSS QSPEQAHLLE
SAILYTRYQS RDFKEGVKSF LEKRKPRFQD TMREQSGEGV LERGDCVVGL ASKPKL
