AKT41_ALTAL
ID AKT41_ALTAL Reviewed; 423 AA.
AC V5XYR2;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Hydroxymethylglutaryl-CoA synthase-like protein AKT4-1 {ECO:0000305};
DE EC=2.3.3.- {ECO:0000305};
DE AltName: Full=AK-toxin biosynthesis protein 4-1 {ECO:0000303|Ref.1};
GN Name=AKT4-1 {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].
RC STRAIN=15A;
RA Mase R., Tanaka A., Harimoto Y., Tsuge T.;
RT "The gene cluster involved in AK-toxin biosynthesis of Alternaria
RT alternata.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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=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 [4]
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 [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).
RN [6]
RP FUNCTION, AND PATHWAY.
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: Hydroxymethylglutaryl-CoA synthase-like protein; part of the
CC gene clusters that mediate the biosynthesis of the host-selective
CC toxins (HSTs) AK-toxins responsible for Japanese pear black spot
CC disease by the Japanese pear pathotype (PubMed:24611558). AK-toxins are
CC esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA)
CC (PubMed:22846083). On cellular level, AK-toxins affect plasma membrane
CC of susceptible cells and cause a sudden increase in loss of K(+) after
CC a few minutes of toxin treatment (PubMed:22846083). The acyl-CoA ligase
CC AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved
CC in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-
CC hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety
CC (PubMed:10432635, PubMed:10975654, PubMed:22846083). Part of the EDA
CC biosynthesis occurs in the peroxisome since these 3 enzymes are
CC localized in peroxisomes (PubMed:20348386). The exact roles of the 3
CC enzymes, as well as of additional AK-toxin clusters enzymes, including
CC AKT4, AKT6 and AKTS1, have still to be elucidated (PubMed:10432635,
CC PubMed:10975654, PubMed:22846083). The Cytochrome P450 monooxygenase
CC AKT7 on the other side functions to limit production of EDA and AK-
CC toxin, probably via the catalysis of a side reaction of EDA or its
CC precursor (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:0000305|PubMed:24611558}.
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 thiolase-like superfamily. HMG-CoA synthase
CC family. {ECO:0000305}.
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DR EMBL; AB872927; BAO10625.1; -; Genomic_DNA.
DR AlphaFoldDB; V5XYR2; -.
DR SMR; V5XYR2; -.
DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IEA:InterPro.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR000590; HMG_CoA_synt_AS.
DR InterPro; IPR013746; HMG_CoA_synt_C_dom.
DR InterPro; IPR013528; HMG_CoA_synth_N.
DR InterPro; IPR010122; HMG_CoA_synthase_euk.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08540; HMG_CoA_synt_C; 1.
DR Pfam; PF01154; HMG_CoA_synt_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01833; HMG-CoA-S_euk; 1.
DR PROSITE; PS01226; HMG_COA_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Transferase.
FT CHAIN 1..423
FT /note="Hydroxymethylglutaryl-CoA synthase-like protein
FT AKT4-1"
FT /id="PRO_0000444868"
SQ SEQUENCE 423 AA; 47372 MW; 349FE6B860F0F9C5 CRC64;
MSFCDDREGQ RALRILQARL IRSPDACSFA LTAVSSLLRK YSIDPRRIGR LEVGTESLVD
KSKSIKSFVM QLFEESGNFD IEGVDTVNAC YGGTNALFNA VNWVESSAWD GRDAIVVASD
ISLYGKGNAR PTGGAGCVAM LVGPDAPIAF EPGRRGSYMA HTYDFYKPDF TTEYPYINGK
HSIECYIQAV EACYRAYTKR ERRATERLEE ERPDHQAGYE TPLDRFDYLC FHSPTNKLVS
KSYARLLYVD YLENPANPIF AEVPDSIREV EYRASLTDKS IEKTFMGLAQ ERFARCVQPS
TEIPNMCGNM YSASVYGSLC SLLCNVNSET LLGKRITIFS YGSGLASSMF SLKVRGSTKQ
MAEKLDVHRR LVDRVVVSPE DVRERAYLKK CFKPKGGAGP IPADVYSLAE VDELFRRVYT
VKS
