AKT7_ALTAL
ID AKT7_ALTAL Reviewed; 522 AA.
AC V5XZS6;
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=Cytochrome P450 monooxygenase AKT7 {ECO:0000303|PubMed:24611558};
DE EC=1.-.-.- {ECO:0000305|PubMed:24611558};
DE AltName: Full=AK-toxin biosynthesis protein 7 {ECO:0000303|PubMed:24611558};
GN Name=AKT7 {ECO:0000303|PubMed:24611558};
GN Synonyms=AKT7-1 {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], FUNCTION, DISRUPTION PHENOTYPE, AND
RP 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).
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).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene clusters that
CC mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins
CC responsible for Japanese pear black spot disease by the Japanese pear
CC 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=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:24611558}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Increases the production of AK-toxin I and does
CC not affect the virulence to Japanese pear leaves.
CC {ECO:0000269|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 cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB872924; BAO10618.1; -; Genomic_DNA.
DR AlphaFoldDB; V5XZS6; -.
DR SMR; V5XZS6; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..522
FT /note="Cytochrome P450 monooxygenase AKT7"
FT /id="PRO_0000444820"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 452
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 522 AA; 58179 MW; DADC48C3616C869B CRC64;
MKTTIDMQVL YVTCTVLAAL ILGYIQAMII YRLWFHPLSK YPGPWLARIS NLYSAYYAWS
GDLHIDMWRC HQKYGDFVRY APNRLLVNTN TGLKAIYGFN KHVQKSTTYN VMVHRAPSSL
TMTDPQESAQ RRRIVGQGFS STAINQYESI IMEHVQRLAT QLVRRGSDRG SGWSAAQNMS
DWGNHFSFDV ISDIVFGARH ETIGKPDNRY VLGCIDGANI RTSVLFQAAE LTFGRVDRYL
FPKSIESRNR FTPFVSSLVR TRLQSHDASR NDAFSLLVRA KDPETSEGLS MDAIGGECTT
LVMAGSDITS TVIASTLFYL STHTESYDRV KSELQQAFPT ADDVRLGHRL NSCRYLRACI
EESLRLSPPV GGAPWRRVVS DGLLVDGQSI PAGCDVGTSV YALHHNSAYF KAPFVFRPSR
WLTDSGAQGR ESRDIRLAQS AFAPFSIGPR SCLGKGMAYA ELTLVLATLL SKYDMRAAEG
PMRGIGGGRV GAPWGRHREN EFQLTGHVTS AKTGPYVEFK KS
