ID   CTB7_CERBT              Reviewed;         419 AA.
AC   A0A2G5ICC7;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Monooxygenase CTB7 {ECO:0000303|PubMed:29844193};
DE            EC=1.-.-.- {ECO:0000250|UniProtKB:A0ST45};
DE   AltName: Full=Cercosporin toxin biosynthesis cluster protein 7 {ECO:0000303|PubMed:29844193};
GN   Name=CTB7 {ECO:0000303|PubMed:29844193}; ORFNames=CB0940_00836;
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=09-40;
RX   PubMed=29844193; DOI=10.1073/pnas.1712798115;
RA   de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA   Spanner R.E., Neubauer J.D., Jurick W.M. II, Stott K.A., Secor G.A.,
RA   Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT   "Gene cluster conservation provides insight into cercosporin biosynthesis
RT   and extends production to the genus Colletotrichum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E5459-E5466(2018).
RN   [2]
RP   REVIEW ON CERCOSPORIN.
RX   PubMed=11701851; DOI=10.1146/annurev.phyto.38.1.461;
RA   Daub M.E., Ehrenshaft M.;
RT   "The photoactivated cercospora toxin cercosporin: contributions to plant
RT   disease and fundamental biology.";
RL   Annu. Rev. Phytopathol. 38:461-490(2000).
CC   -!- FUNCTION: Monooxygenase; part of the gene cluster that mediates the
CC       biosynthesis of cercosporin, a light-activated, non-host-selective
CC       toxin (By similarity). The perylenequinone chromophore of cercosporin
CC       absorbs light energy to attain an electronically-activated triplet
CC       state and produces active oxygen species such as the hydroxyl radical,
CC       superoxide, hydrogen peroxide or singlet oxygen upon reaction with
CC       oxygen molecules (PubMed:11701851). These reactive oxygen species cause
CC       damage to various cellular components including lipids, proteins and
CC       nucleic acids (PubMed:11701851). The first step of cercosporin
CC       biosynthesis is performed by the polyketide synthase CTB1 which
CC       catalyzes the formation of nor-toralactone (By similarity). The starter
CC       unit acyltransferase (SAT) domain of CTB1 initiates polyketide
CC       extension by the selective utilization of acetyl-CoA, which is
CC       elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain
CC       by successive condensations with six malonyl units introduced by the
CC       malonyl acyltransferase (MAT) domain. The product template (PT) domain
CC       catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a
CC       trihydroxynaphthalene, which is thought to be delivered to the
CC       thioesterase (TE) domain for product release (By similarity). The
CC       bifunctional enzyme CTB3 then methylates nor-toralactone to toralactone
CC       before conducting an unusual oxidative aromatic ring opening (By
CC       similarity). The O-methyltransferase CTB2 further methylates the
CC       nascent OH-6 of the CBT3 product, blocking further oxidation at this
CC       site before the reductase CTB6 reduces the 2-oxopropyl ketone at
CC       position C7, giving naphthalene (By similarity). The FAD-dependent
CC       monooxygenase CTB5 in concert with the multicopper oxidase CTB12 are
CC       responsible for homodimerization of naphthalene with CTB7 installing
CC       the dioxepine moiety, finally producing cercosporin (By similarity).
CC       The fasciclin domain-containing protein CTB11 might act with CTB5 and
CC       CTB12 whereas the roles of CTB9 and CTB10 have still to be elucidated
CC       (By similarity). {ECO:0000250|UniProtKB:A0ST45,
CC       ECO:0000250|UniProtKB:Q0UHZ9, ECO:0000303|PubMed:11701851}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:A0ST45}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000305}.
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DR   EMBL; LKMD01000100; PIB02400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5ICC7; -.
DR   SMR; A0A2G5ICC7; -.
DR   OrthoDB; 462247at2759; -.
DR   Proteomes; UP000230605; Chromosome 1.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..419
FT                   /note="Monooxygenase CTB7"
FT                   /id="PRO_0000449871"
SQ   SEQUENCE   419 AA;  45616 MW;  17439B57047D1E80 CRC64;
     MASSNRRVLV NGGGPAGAVT AFWLAKGGFE VVVTERSMSR PYGQGVDVTG RASDIIKKMG
     LEQRIRDSTT GEAGLTVVDD QGEDVAPPLG TAPIEGGTAS VTQEIEIMRR DLTKIFVDAA
     EALPNVTFRY GCTVDEVQQH EKSITAVLSD TGKPEDFTAI IGADGLGSAI RKLTFDPEIN
     RRSVSPTNTY VAFFSIPGDP KYDTPVGKLQ HANKGRGILV RPIDKKGTQR SCYLMSQSDS
     QELAQVARTG SQEDQKALLD NRFREFTGPL GKRAVEGMHS ADDFYFTRIV QIKLDSWHSG
     RAALVGDAGY SPSPLTGQGT TLAIIGAYVL AGEMAKSPDD LERAFTSYYA ILNKFVSESQ
     EIPFGGQAPK LILPQSDWGI WLLRTFYKII SWTGIWRLLN FGNETVKVEL PEYDFGGLD