AF101_ALTAL
ID AF101_ALTAL Reviewed; 432 AA.
AC Q50LG2;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Acyl-CoA dehydrogenase AFT10-1 {ECO:0000303|Ref.1};
DE EC=1.-.-.- {ECO:0000305|Ref.1};
DE AltName: Full=AF-toxin biosynthesis protein 10-1 {ECO:0000303|Ref.1};
GN Name=AFT10-1 {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], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
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 [2]
RP FUNCTION.
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 [3]
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 [4]
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 [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: Acyl-CoA dehydrogenase; part of the gene clusters that
CC mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins
CC responsible for Alternaria black spot of strawberry disease by the
CC strawberry pathotype (Ref.1). AF-toxin I and III are valine derivatives
CC of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid
CC respectively, while AF II is an isoleucine derivative of 2-hydroxy-
CC valeric acid (PubMed:15066029, Ref.1, PubMed:22846083). These
CC derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic
CC acid (EDA) moiety (PubMed:15066029, Ref.1, 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.1, 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.1,
CC PubMed:18986255). {ECO:0000269|PubMed:12019223,
CC ECO:0000269|PubMed:15066029, ECO:0000269|PubMed:18986255,
CC ECO:0000269|Ref.1, ECO:0000303|PubMed:22846083}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|RuleBase:RU362125};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: Reduces the production of AF-toxin and
CC pathogenicity. {ECO:0000269|Ref.1}.
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 acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB179766; BAD97695.1; -; Genomic_DNA.
DR AlphaFoldDB; Q50LG2; -.
DR SMR; Q50LG2; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Virulence.
FT CHAIN 1..432
FT /note="Acyl-CoA dehydrogenase AFT10-1"
FT /id="PRO_0000444867"
SQ SEQUENCE 432 AA; 47613 MW; 8B0A344907C89684 CRC64;
MSYFFGSTVP FAEPLWYSRP ENFRYNESHR RLRESVRGYI EAEIMPFCTQ WEADGEVPSH
VLKRHAALGY AAALINPSAV KEHMHDVRLP GDVPPREWDE FHGLIVADEV ARCGSLGVLW
ALGCGTAIAC PILVNYGTEE QKAKFLPPVI HGESRFCLGI TEPEVGSDIA NLVTRAEQEG
NYFIVNGTKK WVTNGTFADY CIAAVRTGQA GRTGISLLNI PLDVAGVSRE KIESSGVASG
GTASITFDNV QVPVENLLGE KNKGFYMLMS SFDHHRSWIA ANCLRLARVC LEDAYQYALT
RQTFGKPLIN HQTIRLKLAN IGIQITSSYA LLESLTEMRQ NLSVKMGQVH RGIGGLCAIT
KVAAARTFEL AVRESQQIMG ASAYTRTGPG LRVERLSRDM RVLVIGGGSE EILSEMSVVQ
EQKDLNRCKS CP
