ID   ACRS1_ALTAL             Reviewed;         375 AA.
AC   L8AXV5;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Cytochrome P450 monooxygenase ACRTS1 {ECO:0000303|PubMed:22779742};
DE            EC=1.-.-.- {ECO:0000305|PubMed:22779742};
DE   AltName: Full=ACR-toxin biosynthesis protein S1 {ECO:0000303|PubMed:22779742};
GN   Name=ACRTS1 {ECO:0000303|PubMed:22779742};
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=HC1;
RX   PubMed=22779742; DOI=10.1094/phyto-02-12-0021-r;
RA   Izumi Y., Kamei E., Miyamoto Y., Ohtani K., Masunaka A., Fukumoto T.,
RA   Gomi K., Tada Y., Ichimura K., Peever T.L., Akimitsu K.;
RT   "Role of the pathotype-specific ACRTS1 gene encoding a hydroxylase involved
RT   in the biosynthesis of host-selective ACR-toxin in the rough lemon
RT   pathotype of Alternaria alternata.";
RL   Phytopathology 102:741-748(2012).
RN   [2]
RP   FUNCTION.
RC   STRAIN=HC1;
RX   PubMed=22835272; DOI=10.1094/mpmi-06-12-0155-r;
RA   Izumi Y., Ohtani K., Miyamoto Y., Masunaka A., Fukumoto T., Gomi K.,
RA   Tada Y., Ichimura K., Peever T.L., Akimitsu K.;
RT   "A polyketide synthase gene, ACRTS2, is responsible for biosynthesis of
RT   host-selective ACR-toxin in the rough lemon pathotype of Alternaria
RT   alternata.";
RL   Mol. Plant Microbe Interact. 25:1419-1429(2012).
RN   [3]
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 cluster that
CC       mediates the biosynthesis of the host-selective toxins (HSTs) ACR-
CC       toxins responsible for brown spot of rough lemon disease by the rough
CC       lemon pathotype (PubMed:22779742). ACR-toxins cause uncoupling of
CC       mitochondrial oxidative-phosphorylation similar to that of classic
CC       protonophore (PubMed:22846083). The structure of the major form of ACR-
CC       toxin (ACR-toxin I) consists of an alpha-dihydropyrone ring in a 19-
CC       carbon polyalcohol, a typical polyketide structure. Minor toxins were
CC       characterized as having a pyrone ring with polyalcohol side chains
CC       different in length and showing weaker toxicity (PubMed:22846083). The
CC       highly reducing polyketide synthase ACRTS2 has all necessary enzymatic
CC       domains for multiple cycles of condensation and beta-keto processing
CC       (PubMed:22779742). The cytochrome P450 monooxygenase ACRTS1 has also
CC       been shown to be essential for ACR-toxin biosynthesis, however its
CC       exact role in the pathway has not been elucidated yet
CC       (PubMed:22779742). {ECO:0000269|PubMed:22779742,
CC       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:22779742}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of ACR-toxin and impairs
CC       the pathogenicity (PubMed:22779742). Does not affect growth rate of
CC       cultures, sporulation, and spore germination (PubMed:22779742).
CC       {ECO:0000269|PubMed:22779742}.
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:22779742). The CDCs are not essential for saprophytic growth
CC       but controls host-selective pathogenicity (PubMed:22779742). Although
CC       conventional disruption of ACRTS1 could not be accomplished due to the
CC       high number of the copies identified in the genome, the high sequence
CC       identity among these copies of ACRTS1 is likely an advantage for RNA
CC       silencing, because it allows knockdown of all copies of this gene
CC       simultaneously (PubMed:22779742). {ECO:0000269|PubMed:22779742}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB688098; BAM74416.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8AXV5; -.
DR   SMR; L8AXV5; -.
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; Metal-binding; Monooxygenase; Oxidoreductase; Virulence.
FT   CHAIN           1..375
FT                   /note="Cytochrome P450 monooxygenase ACRTS1"
FT                   /id="PRO_0000444819"
FT   BINDING         321
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   375 AA;  41883 MW;  631E5F730A248DA3 CRC64;
     MRKVVGSAYT LTSMLKNEGA LDEVVELFME KLGGFADEQA AFDFGEWLEM FSFDGVGTVF
     FGSPFGFIKD SIDYGGYINA VHTAMPLNSV VAMAPLWLRP VILYGGIAVP RIFKAIMAAD
     GIRKTAVRVT EIAQARSTDS TSRRTDILSR ILSIKDERPG SLTINDVHVE MWGAVIAGSD
     STSGALRAIF YYLMKTPDTM TRLVKEIDAA FANGSLTHPI RYSQAIKLAY LDAVIQESLR
     VFPPFAVPMP RYAPAGGLEI SGHYLKSGTK IGMNAMVVQF NKEVFGEDAH KFRPERWLES
     KDRYRAMNKA MLVFGAGTRT CIGKHLSKAE MYKVVPEILR RFTVRMAHDQ PWKTRNATFI
     MQSNVVCRLE RRSDE