CLAC_PASFU
ID CLAC_PASFU Reviewed; 267 AA.
AC P0CU75;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Short chain dehydrogenase claC {ECO:0000303|PubMed:27274078};
DE EC=1.1.1.- {ECO:0000269|PubMed:27274078};
DE AltName: Full=Cladofulvin biosynthesis cluster protein C {ECO:0000303|PubMed:27274078};
GN Name=claC {ECO:0000303|PubMed:27274078}; ORFNames=Clafu184391;
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, AND INDUCTION.
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 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: Non-reducing polyketide synthase; 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 monooxygenase P450 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). 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; P0CU75; -.
DR SMR; P0CU75; -.
DR OMA; NAAHAHR; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..267
FT /note="Short chain dehydrogenase claC"
FT /id="PRO_0000445895"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 19..27
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 46..47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 72..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 164..168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 197..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 267 AA; 28549 MW; F10D10FF66DCF890 CRC64;
MAVVNGNYIP GRLDGRVAVV TGSGRGIGAA IAVHLGRLGA NIVVNYANSA LDAQKVVDQI
KGAGSEAIAI KADIRDVSQI MRLFDEAVAH FGHVDIAVSN SGVVSFGHLK DVTEEEFDRV
FSLNTRGQFF VAREAYRHLS EGGRIIMTSS NTSKDFSVPR HSLYSGSKGA VDSFVRIFSK
DCGDKKITVN GVAPGGTVTD MFHDVSHHYI PDGEKYTAEQ RQQMAAFASP LHRNGFPEDI
ANVVGFLASK EGEWINGKVI NLDGGAA
