ID   CLAB_PASFU              Reviewed;         162 AA.
AC   P0CU74;
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=Scytalone dehydratase-like protein claB {ECO:0000303|PubMed:27274078};
DE            EC=4.2.1.- {ECO:0000269|PubMed:27274078};
DE   AltName: Full=Cladofulvin biosynthesis cluster protein B {ECO:0000303|PubMed:27274078};
GN   Name=claB {ECO:0000303|PubMed:27274078}; ORFNames=Clafu184392;
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, AND FUNCTION.
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, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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: Scytalone dehydratase-like protein; part of the gene cluster
CC       that mediates the biosynthesis of the bianthraquinone cladofulvin, a
CC       conidial pigment not required for virulence but that plays a role in
CC       fitness and resistance to environmental stresses including UV light and
CC       low-temperature stress (PubMed:24465762, PubMed:27274078). The pathway
CC       begins with the synthesis of atrochrysone thioester by the polyketide
CC       synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF
CC       then breaks the thioester bond and releases the atrochrysone carboxylic
CC       acid from claG (PubMed:27274078). This compound is decarboxylated by
CC       claH to yield emodin, which is further converted to chrysophanol
CC       hydroquinone by the reductase claC and the dehydratase claB
CC       (PubMed:27274078). The cytochrome P450 monooxygenase claM then
CC       catalyzes the dimerization of nataloe-emodin to cladofulvin
CC       (PubMed:27274078). {ECO:0000269|PubMed:24465762,
CC       ECO:0000269|PubMed:27274078}.
CC   -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:27274078}.
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). {ECO:0000269|PubMed:24521437,
CC       ECO:0000269|PubMed:27274078, ECO:0000269|PubMed:27997759}.
CC   -!- SIMILARITY: Belongs to the scytalone dehydratase family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CU74; -.
DR   SMR; P0CU74; -.
DR   OMA; ARIKTQH; -.
DR   GO; GO:0030411; F:scytalone dehydratase activity; IEA:InterPro.
DR   GO; GO:0006582; P:melanin metabolic process; IEA:InterPro.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR004235; Scytalone_dehydratase.
DR   Pfam; PF02982; Scytalone_dh; 1.
DR   PIRSF; PIRSF024851; SCD1; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
PE   1: Evidence at protein level;
KW   Lyase.
FT   CHAIN           1..162
FT                   /note="Scytalone dehydratase-like protein claB"
FT                   /id="PRO_0000445894"
FT   ACT_SITE        83
FT                   /evidence="ECO:0000250|UniProtKB:P56221"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000250|UniProtKB:P56221"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P56221"
SQ   SEQUENCE   162 AA;  18617 MW;  03E5BFB36F836722 CRC64;
     MTRQAVPKPA YEDLVDCQSA MFEWAESFDS KDWDRLSACL APTLFLDYSD IMGKKWDALP
     VEEFIGMASS PHFLGNARIK TQHFIGASKW TQPDEGQIVG FHQMRVAHQK YGDDELKQVL
     YHGHAHGKAT TYYRNVGGQW KFAGLVPDVR WTEFDCDKIF EH