PIG12_CLAP2
ID PIG12_CLAP2 Reviewed; 141 AA.
AC M1W271;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Decarboxylase CPUR_05434 {ECO:0000303|PubMed:28955461};
DE EC=4.1.1.- {ECO:0000305|PubMed:28955461};
DE AltName: Full=Ergochrome gene cluster protein CPUR_05434 {ECO:0000303|PubMed:28955461};
GN ORFNames=CPUR_05434;
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: Decarboxylase; part of the ergochrome gene cluster
CC responsible for the typical purple-black color of the ergot sclerotia
CC (PubMed:28955461). The ergochrome gene cluster produces several ergot
CC pigments including the yellow ergochrome secalonic acid and its
CC 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 decarboxylase CPUR_05434 then
CC catalyzes the concerted decarboxylation-elimination required to convert
CC atochrysone carboxylic acid into emodin anthrone, which is further
CC oxidized to emodin by the anthrone oxygenase CPUR_05435 (By
CC similarity). Emodin is further modified to yield monodictyphenone via
CC several steps involving CPUR_05427, CPUR_05428, CPUR_05429 and
CC CPUR_05430 (By similarity). The short chain dehydrogenase/reductase
CC CPUR_05418 then catalyzes the C-5 ketoreduction to give the xanthone
CC skeleton of the monomeric units (PubMed:32105084). Ergochromes
CC formation requires further dimerization steps of different xanthone
CC 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}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=atrochrysone carboxylate + H(+) = atrochrysone + CO2;
CC Xref=Rhea:RHEA:64264, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:149713, ChEBI:CHEBI:150016;
CC Evidence={ECO:0000305|PubMed:28955461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64265;
CC Evidence={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 tpcK family. {ECO:0000305}.
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DR EMBL; CAGA01000032; CCE31581.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W271; -.
DR EnsemblFungi; CCE31581; CCE31581; CPUR_05434.
DR VEuPathDB; FungiDB:CPUR_05434; -.
DR eggNOG; ENOG502SJ0E; Eukaryota.
DR HOGENOM; CLU_115019_0_0_1; -.
DR OrthoDB; 1621831at2759; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR009799; EthD_dom.
DR Pfam; PF07110; EthD; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
PE 2: Evidence at transcript level;
KW Lyase; Reference proteome.
FT CHAIN 1..141
FT /note="Decarboxylase CPUR_05434"
FT /id="PRO_0000443978"
FT DOMAIN 26..121
FT /note="EthD"
FT /evidence="ECO:0000255"
SQ SEQUENCE 141 AA; 16769 MW; 66496731CFB2093A CRC64;
MKMGMAKHSP RNKEYLCLTI CGYRKEGMSE EAYRNHMVNV SAPMTKDLMV KYGIRRWTQI
HNQNATRALM AELFDPQMCR LADFDCFSQV VFDNIEDYKR MKQDPWYKKH LMHDHEMFAD
TKRSMMTIGW IKEFVVDGKA V