PIG7_CLAP2
ID PIG7_CLAP2 Reviewed; 264 AA.
AC M1W270;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Short chain dehydrogenase CPUR_05429 {ECO:0000303|PubMed:28955461};
DE EC=1.1.1.- {ECO:0000305|PubMed:28955461};
DE AltName: Full=Ergochrome gene cluster protein CPUR_05429 {ECO:0000303|PubMed:28955461};
GN ORFNames=CPUR_05429;
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, AND INDUCTION.
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 FUNCTION.
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; part of the ergochrome gene
CC cluster responsible for the typical purple-black color of the ergot
CC sclerotia (PubMed:28955461). 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:Q5BH34, ECO:0000269|PubMed:28955461,
CC ECO:0000269|PubMed:32105084}.
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000305|PubMed:28955461}.
CC -!- INDUCTION: Expression correlates with the formation of the sclerotia
CC and thus the pigment production and is directly regulated by the
CC cluster-specific activator CPUR_05433 (PubMed:28955461).
CC {ECO:0000269|PubMed:28955461}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAGA01000032; CCE31576.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W270; -.
DR SMR; M1W270; -.
DR STRING; 1111077.M1W270; -.
DR EnsemblFungi; CCE31576; CCE31576; CPUR_05429.
DR VEuPathDB; FungiDB:CPUR_05429; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR OrthoDB; 913128at2759; -.
DR PhylomeDB; M1W270; -.
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; 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 2: Evidence at transcript level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..264
FT /note="Short chain dehydrogenase CPUR_05429"
FT /id="PRO_0000443980"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 16..24
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 43..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 69..71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 161..165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 194..196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 264 AA; 28124 MW; 13DC57ADEEB8D37B CRC64;
MSETHIPYRL DGKIALVTGS GRGIGAAMAV ELGRLGAKVV VNYVNSVESA EKVVDEIKGL
GSDAVAIQAD VRQVSQIVEL MDKAVKHFGG LDIVCSNSGV VSFGHFGDVT EEEFDRVFSL
NTRGQFFVAR EAYRHLNNGG RIILMSSNTA KDLSVPKHSL YSGSKGAIDS FVRIFSKDAG
DKKITVNAVA PGGTVTDMFH SCSQHYIPGG DKYTAEERQA MAAHASPLTR NGFPLDIAKV
VCFLASDEAE WVNGKVLTLD GGAA
