ID   CTB5_CERBT              Reviewed;         527 AA.
AC   A0A2G5ICA0;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=FAD-dependent monooxygenase CTB5 {ECO:0000303|PubMed:29844193};
DE            EC=1.-.-.- {ECO:0000250|UniProtKB:A0ST43};
DE   AltName: Full=Cercosporin toxin biosynthesis cluster protein 5 {ECO:0000303|PubMed:29844193};
GN   Name=CTB5 {ECO:0000303|PubMed:29844193}; ORFNames=CB0940_00835;
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: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of cercosporin, a light-activated, non-host-
CC       selective toxin (By similarity). The perylenequinone chromophore of
CC       cercosporin absorbs light energy to attain an electronically-activated
CC       triplet state and produces active oxygen species such as the hydroxyl
CC       radical, superoxide, hydrogen peroxide or singlet oxygen upon reaction
CC       with oxygen molecules (PubMed:11701851). These reactive oxygen species
CC       cause damage to various cellular components including lipids, proteins
CC       and 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:A0ST43,
CC       ECO:0000250|UniProtKB:Q0UHZ9, ECO:0000303|PubMed:11701851}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:A0ST43}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; LKMD01000100; PIB02399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5ICA0; -.
DR   SMR; A0A2G5ICA0; -.
DR   OrthoDB; 733611at2759; -.
DR   Proteomes; UP000230605; Chromosome 1.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..527
FT                   /note="FAD-dependent monooxygenase CTB5"
FT                   /id="PRO_0000449869"
FT   DOMAIN          78..255
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   527 AA;  57820 MW;  718C3C967F8932B2 CRC64;
     MLGLNLQQVL SNVPTISSIV SGVGSYQHGS DSSAWASVAA SKSCCDALTK SLGKNSVVFP
     YDAAYSQSMG SYFSLKNSDL HPSCIALPRS AEDVSKAVRT LSLGAHKWEG QCQFGVRGGG
     HTPFKGAAST DNGIVLDLLH MPSAGISPDY ETITVSPSTT WDLVYEVLDA HNRSTLGTKV
     AGIGVGGAST SCGVSYFSPR YGYICDMVEN WEVVLATGDI VNANANENPD LWKALRGGIN
     NFGIVTAVTL KTFGQGPFWG GQTFHSIDTR QEHFKNHEKL ASAHPYDPYA HYINTLVWAN
     GGHWFIGNSI QYTKSDPPVA EPEVFKPFLK TERTPIFPGL PEDTLRVDNV TSFSREYAAN
     TLYPQRWQFA CISFAPDADF METFFQMAND AMQQYVKLAG FKLILNYQPA PTVQLERNGA
     VDSLGPIQTE GNVVFVHWAV SYDESEAQFD DAITKSVQDL FHAANAKAKE LGIYRHFIQP
     TYADSWQSPF DYRSKSTIEE LVATSKKYDP LQVFQKQVPG GFKLPQI