AKS11_ALTAL
ID AKS11_ALTAL Reviewed; 409 AA.
AC V5Y0V0;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Threonine dehydratase-like protein AKTS1-1 {ECO:0000305};
DE EC=4.3.1.- {ECO:0000305};
DE AltName: Full=AK-toxin biosynthesis protein S1-1 {ECO:0000303|PubMed:24611558};
GN Name=AKTS1-1 {ECO:0000303|PubMed:24611558};
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: Threonine dehydratase-like protein; part of the gene clusters
CC that mediate the biosynthesis of the host-selective toxins (HSTs) AK-
CC toxins responsible for Japanese pear black spot disease by the Japanese
CC pear pathotype (PubMed:24611558). AK-toxins are esters of 9,10-epoxy 8-
CC hydroxy 9-methyldecatrienoic acid (EDA) (PubMed:22846083). On cellular
CC level, AK-toxins affect plasma membrane of susceptible cells and cause
CC a sudden increase in loss of K(+) after a few minutes of toxin
CC treatment (PubMed:22846083). The acyl-CoA ligase AKT1, the hydrolase
CC AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis
CC of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-
CC 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P04968};
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 serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; AB872926; BAO10624.1; -; Genomic_DNA.
DR AlphaFoldDB; V5Y0V0; -.
DR SMR; V5Y0V0; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Virulence.
FT CHAIN 1..409
FT /note="Threonine dehydratase-like protein AKTS1-1"
FT /id="PRO_0000444861"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT BINDING 239..243
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT BINDING 368
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT MOD_RES 111
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04968"
SQ SEQUENCE 409 AA; 44959 MW; D86ED1E1D4FCFB3D CRC64;
MADYLRQVMP ENDSDSEALP RKSEQASLAW AEYTANFEMG LESSKLKNNK NMPEAFLLPN
GYPDYLRLIL TSRVYDVVTE TPLTPVVNIS NRLGCKVLLK REDLQPVFSF KLRGAYNKMA
HLDPRDCWRG VVTYSTGNHA QGVAYSARKL RIPATIVMPS GTPDIMHMNV SRLGGSVILH
GADLDTAKAE AERLEKIYNL ISIPPLDDPY VIAGHGTIGM ELLHQISSKN LEAVFCCAGE
GSLIAGIGIY LKRIAPHVNI IGVEMHNPKA TVKSLEGVKY TTLKDAGLFA RCATVKTAGR
ESYRIFQEVV SEVIEVTMDE TFGATKDIFE DTRAIIEPAG ALVLAGLKKW VSQNPSVNQD
RCLVAIASGA NVDFDHLRLI TERASIAENK GGLHEINGVS RNEEPYLLS
