AFT11_ALTAL
ID AFT11_ALTAL Reviewed; 578 AA.
AC Q96VB5;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Acyl-CoA ligase AFT1-1 {ECO:0000303|PubMed:12019223};
DE EC=6.2.1.- {ECO:0000305|PubMed:12019223};
DE AltName: Full=AF-toxin biosynthesis protein 1-1 {ECO:0000303|PubMed:12019223};
GN Name=AFT1-1 {ECO:0000303|PubMed:12019223};
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 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 [3]
RP 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 [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 ligase; part of the gene clusters that mediate the
CC biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible
CC for Alternaria black spot of strawberry disease by the strawberry
CC pathotype (PubMed:12019223). 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.3, PubMed:22846083). These
CC derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic
CC acid (EDA) moiety (PubMed:15066029, Ref.3, 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.3, PubMed:18986255). The exact role of
CC each enzyme, and of additional enzymes identified within the AF-toxin
CC clusters have still to be determined (PubMed:12019223, Ref.3,
CC PubMed:18986255). {ECO:0000269|PubMed:12019223,
CC ECO:0000269|PubMed:15066029, ECO:0000269|PubMed:18986255,
CC ECO:0000269|Ref.3, ECO:0000303|PubMed:22846083}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:12019223}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O93800}.
CC Note=The peroxisomal location requires the C-terminal tripeptide
CC peroxisomal targeting signal. {ECO:0000250|UniProtKB:O93800}.
CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity. {ECO:0000250|UniProtKB:Q42524}.
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, 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 ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB070711; BAB69076.1; -; Genomic_DNA.
DR AlphaFoldDB; Q96VB5; -.
DR SMR; Q96VB5; -.
DR PHI-base; PHI:508; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Peroxisome; Virulence.
FT CHAIN 1..578
FT /note="Acyl-CoA ligase AFT1-1"
FT /id="PRO_0000444859"
FT REGION 281..350
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 351..413
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT MOTIF 576..578
FT /note="Peroxisomal targeting signal type 1"
FT /evidence="ECO:0000250|UniProtKB:O93800"
FT BINDING 210..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 350..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ SEQUENCE 578 AA; 63213 MW; B8B07A507DC53145 CRC64;
MVFTAPCWVP PLPSDLPDST TLEEFIFCQV KDSQTRSELD RSILICGTQG REYTVQESME
RTGRLAQGLS AWLNWPQKSP GKDWKVAAIF NVNCVDFFSI SHAIHRLGGT ISAINASSTA
DELEAQLRLS NAQAIFTCNT LLKIAMKASQ RVGIPLANIF LTDAPGSYRP DDVYPFQEID
NIVRTAKSSL PLLQLGRGQG ASTPAYICFS SGTSGAQKPV LLSHQGIIAN IVQINTFEKF
RQKGPNISLC ILPLAHSYGL VCVAYSALYR GDRLAVLPSS GVEDLLSIVE KLKINTLYLV
PTLVSRILSG GKAGRHDLRC VKEVYTGGAP LHPMLGEHIL RHHPTWKIKQ CYGATEAGTA
VSVTSDCDLW PGSVGCLLPG VQAKIVKSDG SETTKHDESG ELWVSSPSLA IGYLSNPLAT
KTTFTVDNTG KTWLRTGDEV KICLSPNGNE HLFIVDRIKD IIKVKGFQVA PVELEQLLLS
NDFVEEVAVT SRQDEGEEER PQAFVVRSQV GLEEPQGAVA ESLHALVKAR KARYKWLHPH
VIFVDSLPKT TSGKIMRRAL RNMSPANSEV NSRLSSKI
