PIG17_CLAP2
ID PIG17_CLAP2 Reviewed; 292 AA.
AC M1W848;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Short chain dehydrogenase/reductase CPUR_05418 {ECO:0000303|PubMed:30996871};
DE Short=SDR CPUR_05418 {ECO:0000303|PubMed:30996871};
DE EC=1.1.1.- {ECO:0000269|PubMed:32105084};
DE AltName: Full=Ergochrome biosynthesis cluster protein CPUR_05418 {ECO:0000303|PubMed:30996871};
GN ORFNames=CPUR_05418;
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1;
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
RN [2]
RP FUNCTION.
RX PubMed=28955461; DOI=10.1186/s40694-016-0020-z;
RA Neubauer L., Dopstadt J., Humpf H.U., Tudzynski P.;
RT "Identification and characterization of the ergochrome gene cluster in the
RT plant pathogenic fungus Claviceps purpurea.";
RL Fungal Biol. Biotechnol. 3:2-2(2016).
RN [3]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=30996871; DOI=10.1039/c8sc05126g;
RA Greco C., de Mattos-Shipley K., Bailey A.M., Mulholland N.P., Vincent J.L.,
RA Willis C.L., Cox R.J., Simpson T.J.;
RT "Structure revision of cryptosporioptides and determination of the genetic
RT basis for dimeric xanthone biosynthesis in fungi.";
RL Chem. Sci. 10:2930-2939(2019).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=32105084; DOI=10.1021/acs.orglett.0c00285;
RA Wei X., Matsuda Y.;
RT "Unraveling the fungal strategy for tetrahydroxanthone biosynthesis and
RT diversification.";
RL Org. Lett. 22:1919-1923(2020).
CC -!- FUNCTION: Short chain dehydrogenase/reductase; part of the ergochrome
CC gene cluster responsible for the typical purple-black color of the
CC ergot sclerotia (Probable). The ergochrome gene cluster produces
CC several ergot pigments including the yellow ergochrome secalonic acid
CC and its derivatives, as well as the red anthraquinones endocrocin and
CC clavorubin (PubMed:28955461). The pathway begins with the synthesis of
CC atrochrysone thioester by the polyketide synthase (PKS) CPUR_05437 (By
CC similarity). The atrochrysone carboxyl ACP thioesterase CPUR_05436 then
CC breaks the thioester bond and releases the atrochrysone carboxylic acid
CC from CPUR_05437 (By similarity). The atrochrysone carboxylic acid is
CC then converted to atrochrysone which is further transformed into emodin
CC anthrone (By similarity). The next step is performed by the anthrone
CC oxygenase CPUR_05434 that catalyzes the oxidation of emodinanthrone to
CC emodin (By similarity). Emodin is further modified to yield
CC monodictyphenone via several steps involving CPUR_05427, CPUR_05428,
CC CPUR_05429 and CPUR_05430 (By similarity). The short chain
CC dehydrogenase/reductase CPUR_05418 then catalyzes the C-5 ketoreduction
CC to give the xanthone skeleton of the monomeric units (PubMed:32105084).
CC Ergochromes formation requires further dimerization steps of different
CC xanthone units, probably catalyzed by the cytochrome P450 monooxygenase
CC CPUR_05419 (PubMed:28955461). CPUR_05425, CPUR_05426 and CPUR_05431 are
CC unique to Claviceps, thus it is likely that they are involved in
CC further modification of xanthone units or in their dimerization
CC (PubMed:28955461). The yellow ergochromes and the red anthraquinone
CC pigments endocrocin and clavorubin are products from the same PKS
CC derived precursors and the latter are likely shunt products in the
CC pathway of xanthone biosynthesis (PubMed:28955461). It is proposed that
CC atrochrysone carboxylic acid released from the PKS CPUR_05437 can also
CC be converted to endocrocin anthrone which is further oxidized into
CC endocrocin by CPUR_05435 (By similarity). Endocrocin could be then
CC modified to clavorubin, possibly by CPUR_05423 and CPUR_05431
CC (PubMed:28955461). Clavorubin is the principal anthraquinone metabolite
CC produced by the cluster with a much higher yield compared to endocrocin
CC (PubMed:28955461). {ECO:0000250|UniProtKB:Q4W944,
CC ECO:0000250|UniProtKB:Q5BH30, ECO:0000269|PubMed:28955461,
CC ECO:0000269|PubMed:32105084, ECO:0000305|PubMed:30996871}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:32105084}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CAGA01000032; CCE31565.1; -; Genomic_DNA.
DR SMR; M1W848; -.
DR EnsemblFungi; CCE31565; CCE31565; CPUR_05418.
DR VEuPathDB; FungiDB:CPUR_05418; -.
DR eggNOG; KOG4169; Eukaryota.
DR HOGENOM; CLU_010194_8_2_1; -.
DR OrthoDB; 1194344at2759; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
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 SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..292
FT /note="Short chain dehydrogenase/reductase CPUR_05418"
FT /id="PRO_0000453454"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q5BEK1"
FT BINDING 43..51
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 70..71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 95..97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 186..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 221..223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 292 AA; 31092 MW; 7AC8583E37D7C69D CRC64;
MASITTTTNF FESIPRPTKT YRSASYDRIS TRHGFNGTGK TVLITGGSSG IGLSIAKAFA
GAGVARIAIL SRSRATQLTA KAEIEAAYPS TSILLFEASV TDADRFASVL EELAGVHVLV
LCAAAVHARV PLAELSGKDV QHVFDTNSVS TVNLARLYTA TPGKDKTILH VSSAVAQMYA
PLRSVYGASK AAAVQAMQHL AREHQGTGDR VRVFSFHPGA ITTPASGAIY TPGAVQWDDA
DLPAHFSLWL AGPESDFLNG RYVWANWDVD ELVALKERLA CDGRFLTIGL VL
