AFT31_ALTAL
ID AFT31_ALTAL Reviewed; 296 AA.
AC Q96VB3;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Enoyl-CoA hydratase AFT3-1 {ECO:0000303|PubMed:12019223};
DE EC=4.2.1.17 {ECO:0000305|PubMed:12019223};
DE AltName: Full=AF-toxin biosynthesis protein 3-1 {ECO:0000303|PubMed:12019223};
GN Name=AFT3-1; Synonyms=AFT3-2, AFT3-3;
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=NAF8;
RX PubMed=12019223; DOI=10.1093/genetics/161.1.59;
RA Hatta R., Ito K., Hosaki Y., Tanaka T., Tanaka A., Yamamoto M.,
RA Akimitsu K., Tsuge T.;
RT "A conditionally dispensable chromosome controls host-specific
RT pathogenicity in the fungal plant pathogen Alternaria alternata.";
RL Genetics 161:59-70(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=NAF8;
RX DOI=10.1007/s10327-004-0170-3;
RA Ruswandi S., Kitani K., Akimitsu K., Tsuge T., Shiraishi T., Yamamoto M.;
RT "Structural analysis of cosmid clone pcAFT-2 carrying AFT10-1 encoding an
RT acyl-CoA dehydrogenase involved in AF-toxin production in the strawberry
RT pathotype of Alternaria alternata.";
RL J. Gen. Plant Pathol. 71:107-116(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NAF8;
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 [4]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=15066029; DOI=10.1111/j.1365-2958.2004.04004.x;
RA Ito K., Tanaka T., Hatta R., Yamamoto M., Akimitsu K., Tsuge T.;
RT "Dissection of the host range of the fungal plant pathogen Alternaria
RT alternata by modification of secondary metabolism.";
RL Mol. Microbiol. 52:399-411(2004).
RN [5]
RP FUNCTION.
RC STRAIN=NAF8;
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 [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: Enoyl-CoA hydratase; part of the gene clusters that mediate
CC the biosynthesis of the host-selective toxins (HSTs) AF-toxins
CC responsible for Alternaria black spot of strawberry disease by the
CC strawberry pathotype (PubMed:12019223). AF-toxin I and III are valine
CC derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric
CC acid respectively, while AF II is an isoleucine derivative of 2-
CC hydroxy-valeric acid (PubMed:15066029, Ref.2, PubMed:22846083). These
CC derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic
CC acid (EDA) moiety (PubMed:15066029, Ref.2, PubMed:22846083). On
CC cellular level, AF-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 aldo-keto reductase AFTS1
CC catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-
CC hydroxy-isovaleric acid (2-HIV) by reduction of its ketone to an
CC alcohol (PubMed:15066029). The acyl-CoA ligase AFT1, the hydrolase AFT2
CC and the enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide
CC synthase AFT9, the acyl-CoA dehydrogenase AFT10, the cytochrome P450
CC monooxygenase AFT11 and the oxidoreductase AFT12 are all involved in
CC the biosynthesis of the AK-, AF- and ACT-toxin common EDA structural
CC moiety (PubMed:12019223, Ref.2, PubMed:18986255). The exact function of
CC each enzyme, and of additional enzymes identified within the AF-toxin
CC clusters have still to be determined (PubMed:12019223, Ref.2,
CC PubMed:18986255). {ECO:0000269|PubMed:12019223,
CC ECO:0000269|PubMed:15066029, ECO:0000269|PubMed:18986255,
CC ECO:0000269|Ref.2, 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:12019223};
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:12019223};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:12019223}.
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 -!- DISRUPTION PHENOTYPE: Abolishes the production of AF-toxins and their
CC precuror 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA); and
CC impairs the pathogenicity (PubMed:12019223). Does not affect growth
CC rate of cultures, sporulation, and spore germination (PubMed:12019223).
CC {ECO:0000269|PubMed:12019223}.
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:12019223). The CDCs are not essential for saprophytic growth
CC but controls host-selective pathogenicity (PubMed:12019223).
CC {ECO:0000269|PubMed:12019223}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AB070713; BAB69078.1; -; Genomic_DNA.
DR EMBL; AB179766; BAD97699.1; -; Genomic_DNA.
DR EMBL; AB872925; BAO10623.1; -; Genomic_DNA.
DR AlphaFoldDB; Q96VB3; -.
DR SMR; Q96VB3; -.
DR PHI-base; PHI:509; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
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 AFT3-1"
FT /id="PRO_0000444830"
FT MOTIF 294..296
FT /note="Peroxisomal targeting signal type 1"
FT /evidence="ECO:0000250|UniProtKB:Q9P4U9"
SQ SEQUENCE 296 AA; 32131 MW; 5D20668755312F55 CRC64;
MLNRFSYSSN AWHNLRVDGP DADGIAVIVL ARSQSRNALT LPMLTDMVQL LSAMDADDSV
KCIVFTGEGP FFCSGVDLTE GFGEIGKTRD THRDAGGKLA LAIHNCRKPT IAAINGTAVG
VGITMTLPMS IRIAAKTAKI SFPFVRRGIV ADAASSFYLP RLIGYGRALH LFTTGALYPA
ESGLLHGLFS ETVNAASSTL PRALEVARDI AVNASQVGVY LTRDLVYRSP RSPEQAHLLE
SAALYTRYQS RDFEEGVQSF LEKRKPRFQD TMREQSGEGV LDRGDCVVGL AFKPKL
