AKT1_ALTAL
ID AKT1_ALTAL Reviewed; 578 AA.
AC O93800;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Acyl-CoA ligase AKT1 {ECO:0000303|PubMed:10432635};
DE EC=6.2.1.- {ECO:0000305|PubMed:10432635};
DE AltName: Full=AK-toxin biosynthesis protein 1 {ECO:0000303|PubMed:10432635};
GN Name=AKT1 {ECO:0000303|PubMed:10432635};
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=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 [2]
RP FUNCTION.
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 [3]
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 [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: Acyl-CoA ligase; part of the gene clusters that mediate the
CC biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible
CC for Japanese pear black spot disease by the Japanese pear pathotype
CC (PubMed:10432635, PubMed:20348386). AK-toxins are esters of 9,10-epoxy
CC 8-hydroxy 9-methyldecatrienoic acid (EDA) (PubMed:22846083). On
CC cellular level, AK-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 acyl-CoA ligase AKT1, the
CC hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the
CC biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-
CC 9-methyl-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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:10432635}.
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 AK-toxin and impairs
CC the pathogenicity. {ECO:0000269|PubMed:10432635}.
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}.
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DR EMBL; AB015351; BAA36588.1; -; Genomic_DNA.
DR AlphaFoldDB; O93800; -.
DR SMR; O93800; -.
DR PHI-base; PHI:133; -.
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 4: Predicted;
KW ATP-binding; Ligase; Nucleotide-binding; Peroxisome; Virulence.
FT CHAIN 1..578
FT /note="Acyl-CoA ligase AKT1"
FT /id="PRO_0000444860"
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:0000269|PubMed:20348386"
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; 63348 MW; 27F78E0D369508D1 CRC64;
MVFAAPCWVP PLPSDLPDST TLEEFIFCQV KDSQTRSELD RSILICGTQG KEYTVQESME
RTGRLAQGLS AWLDWPQKPS EEDWKVAAIF NINCVEFFSI SHAIHRLGGT VSAINASSTA
DELEAQLRLS NAQAIFTCNT LLKIAMKASQ KVGIPLANIF LTDAPGSYRP DDVYPFQEID
NIVRTARSSL PLLQLGRGQG SSTPAYICFS SGTSGAQKPV LLSHQGIIAN IVQINTFEKF
RQKGPNVSLC ILPLAHSYGL VCVAYNALYR GDRLAVLPSS DVEDLLSIVE KLRINTLYLV
PTLLSRILSG GKAGGHDLSC VKEVYTGGAP LHPMLGEHIL RHHPTWKTKQ CYGATEAGTA
VSVTSDCDLW PGSVGCLLPG VQAKIIRSDG SETTKHDESG ELWVSSPSLA IGYLSNPLAT
EATFTVDNTG RTWLRTGDEA KICLSPNGNE HLFIVDRIKD IIKVKGFQVA PVELEQLLLS
NDFVEEVAIT SRQDKRGEER PQAFVVRTHE GLKEPQDAVS ESLQALVKAR KARYKWLHPH
VIFVDSLPKT TSGKIMRRAL RNMCPANSEV NGRLSSKI
