CLAN_PASFU
ID CLAN_PASFU Reviewed; 218 AA.
AC P0CU71;
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 claN {ECO:0000303|PubMed:27274078};
DE EC=1.-.-.- {ECO:0000305|PubMed:24465762};
DE AltName: Full=Cladofulvin biosynthesis cluster protein N {ECO:0000303|PubMed:27274078};
GN Name=claN {ECO:0000303|PubMed:27274078}; ORFNames=Clafu184399;
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 P450 monooxygenase 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 short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR AlphaFoldDB; P0CU71; -.
DR SMR; P0CU71; -.
DR OMA; CAGYGIL; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase.
FT CHAIN 1..218
FT /note="Oxidoreductase claN"
FT /id="PRO_0000445891"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 6..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 33..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 58..60
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 148..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 181..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 218 AA; 23048 MW; 836E665B1B289781 CRC64;
MSYTWLITRA SSGRGAAIAL AALEAGHKVI AGARNPAKAS QVRPEIQNQG GTWLRLDDST
ADVRHVIAKA AKEHGLNVLV NNAGGYALRG VLEDFSETEL YQQMETNFFG PIRAIQGALP
WSRAQKPGTI FNISSTSDIT GFTGFSLYAA SKAALEGASE ALYGELALFG IRVLVVQPGA
SRTKFQSAGP RPAVSEACVG TTVDAILQRA VGMAAERR
