ID   CLAK_PASFU              Reviewed;         270 AA.
AC   P0CU69;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Oxidoreductase claK {ECO:0000303|PubMed:27274078};
DE            EC=1.-.-.- {ECO:0000305|PubMed:24465762};
DE   AltName: Full=Cladofulvin biosynthesis cluster protein K {ECO:0000303|PubMed:27274078};
GN   Name=claK {ECO:0000303|PubMed:27274078}; ORFNames=Clafu184397;
OS   Passalora fulva (Tomato leaf mold) (Cladosporium fulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Fulvia.
OX   NCBI_TaxID=5499;
RN   [1]
RP   INDUCTION.
RX   PubMed=24521437; DOI=10.1111/mmi.12535;
RA   Okmen B., Collemare J., Griffiths S., van der Burgt A., Cox R.,
RA   de Wit P.J.;
RT   "Functional analysis of the conserved transcriptional regulator CfWor1 in
RT   Cladosporium fulvum reveals diverse roles in the virulence of plant
RT   pathogenic fungi.";
RL   Mol. Microbiol. 92:10-27(2014).
RN   [2]
RP   IDENTIFICATION, FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=24465762; DOI=10.1371/journal.pone.0085877;
RA   Collemare J., Griffiths S., Iida Y., Karimi Jashni M., Battaglia E.,
RA   Cox R.J., de Wit P.J.;
RT   "Secondary metabolism and biotrophic lifestyle in the tomato pathogen
RT   Cladosporium fulvum.";
RL   PLoS ONE 9:E85877-E85877(2014).
RN   [3]
RP   INDUCTION, AND FUNCTION.
RX   PubMed=27274078; DOI=10.1073/pnas.1603528113;
RA   Griffiths S., Mesarich C.H., Saccomanno B., Vaisberg A., De Wit P.J.,
RA   Cox R., Collemare J.;
RT   "Elucidation of cladofulvin biosynthesis reveals a cytochrome P450
RT   monooxygenase required for anthraquinone dimerization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:6851-6856(2016).
RN   [4]
RP   INDUCTION.
RX   PubMed=27997759; DOI=10.1111/mpp.12527;
RA   Griffiths S., Mesarich C.H., Overdijk E.J.R., Saccomanno B.,
RA   de Wit P.J.G.M., Collemare J.;
RT   "Down-regulation of cladofulvin biosynthesis is required for biotrophic
RT   growth of Cladosporium fulvum on tomato.";
RL   Mol. Plant Pathol. 19:369-380(2018).
CC   -!- FUNCTION: Oxidoreductase; part of the gene cluster that mediates the
CC       biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not
CC       required for virulence but that plays a role in fitness and resistance
CC       to environmental stresses including UV light and low-temperature stress
CC       (PubMed:24465762, PubMed:27274078). The pathway begins with the
CC       synthesis of atrochrysone thioester by the polyketide synthase (PKS)
CC       claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the
CC       thioester bond and releases the atrochrysone carboxylic acid from claG
CC       (PubMed:27274078). This compound is decarboxylated by claH to yield
CC       emodin, which is further converted to chrysophanol hydroquinone by the
CC       reductase claC and the dehydratase claB (PubMed:27274078). The
CC       cytochrome monooxygenase P450 claM then catalyzes the dimerization of
CC       nataloe-emodin to cladofulvin (PubMed:27274078).
CC       {ECO:0000269|PubMed:24465762, ECO:0000269|PubMed:27274078}.
CC   -!- PATHWAY: Pigment biosynthesis. {ECO:0000305|PubMed:24465762}.
CC   -!- INDUCTION: Expression is positively regulated by the transcriptional
CC       regulator wor1 (PubMed:24521437, PubMed:27274078). Expression is down-
CC       regulated during biotrophic growth within tomato leaves
CC       (PubMed:27997759). The expression is induced at later stages of
CC       infection when conidiophores emerge from the plant and produce conidia
CC       (PubMed:24465762). {ECO:0000269|PubMed:24465762,
CC       ECO:0000269|PubMed:24521437, ECO:0000269|PubMed:27274078,
CC       ECO:0000269|PubMed:27997759}.
CC   -!- SIMILARITY: Belongs to the avfA family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CU69; -.
DR   SMR; P0CU69; -.
DR   OMA; AYCRNKA; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF13460; NAD_binding_10; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..270
FT                   /note="Oxidoreductase claK"
FT                   /id="PRO_0000445889"
SQ   SEQUENCE   270 AA;  29610 MW;  B332A0755965A662 CRC64;
     MDSKVTTYAV LGSTGNCGSA LIRNLLGKPQ SRVHAFCRNK KKLLRLIPEI ADSKQVEVFE
     GGMQDHDLLA ACIKNTRAVF MCISTNDNVP GCRLSQDSAI ALVKVMRELG YDKPDGGPNG
     PAPKLLLLSS GTIDPHLSKH LPSLLLWILK RSASHVYADL EKAEEFLRAQ ESWLTTIYIK
     PGALSVDKKR GYELSLTEQK DPVSYLDLSA GMIEAADDPE GRWDLKNISV NCGSTPAGFP
     DGTILCILMG LLRHYFPWTH AYLPMGMGPK