ID PIG15_CLAP2 Reviewed; 1808 AA.
AC M1WG96;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Non-reducing polyketide synthase CPUR_05437 {ECO:0000303|PubMed:28955461};
DE EC=2.3.1.- {ECO:0000305|PubMed:28955461};
DE AltName: Full=Ergochrome gene cluster protein CPUR_05437 {ECO:0000303|PubMed:28955461};
GN ORFNames=CPUR_05437;
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, DISRUPTION PHENOTYPE, 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: Non-reducing polyketide synthase; 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:Q5BH30, ECO:0000269|PubMed:28955461,
CC ECO:0000269|PubMed:32105084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8 H(+) + holo-[ACP] + 8 malonyl-CoA = atrochrysone carboxyl-
CC [ACP] + 8 CO2 + 8 CoA + 2 H2O; Xref=Rhea:RHEA:64232, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:149712;
CC Evidence={ECO:0000305|PubMed:28955461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64233;
CC Evidence={ECO:0000305|PubMed:28955461};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|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 -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (By similarity).
CC {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DISRUPTION PHENOTYPE: Leads to the loss of ergot sclerotia pigmentation
CC via blocking the production of red pigments endocrocin and clavorubin,
CC and of the yellow secalonic acids (PubMed:28955461). Does not affect
CC the ability to infect plants (PubMed:28955461).
CC {ECO:0000269|PubMed:28955461}.
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; CCE31584.1; -; Genomic_DNA.
DR AlphaFoldDB; M1WG96; -.
DR SMR; M1WG96; -.
DR STRING; 1111077.M1WG96; -.
DR VEuPathDB; FungiDB:CPUR_05437; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_1_1; -.
DR OrthoDB; 5396558at2759; -.
DR PhylomeDB; M1WG96; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775:SF53; ATROCHRYSONE CARBOXYLIC ACID SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 1.
PE 2: Evidence at transcript level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..1808
FT /note="Non-reducing polyketide synthase CPUR_05437"
FT /id="PRO_0000443986"
FT DOMAIN 406..840
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 1343..1653
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 1730..1807
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 31..272
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 941..1265
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1343..1494
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1375..1650
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1506..1653
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1659..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 579
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 715
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 758
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 1375
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1564
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 1767
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1808 AA; 196538 MW; C525561550FE6A9A CRC64;
MAIYTPNKSS DANSESSSLR VIFFGNELPN DDLQTHFRRL HTRSKDKNHP LLARFIDEAT
LVLKEEISAL STDLGRLIPT FETVLQWSED ANASLREGLL CGAIDGVLLV VLQLASYICY
HEILTYDKEE CVHIALTGLG IGLLSSTAVS LAPTPSHLPL AGADVVRLAF RLGIHVLGVS
ELLEARDVSG KPASWAYLVQ IADSDAAQAE LDLLYGNAES SANSNKIIIS AVSQTSIVAS
GPPSRLKLLF NKSPLFRNAR STALPVFGGL CHAAHIYGEN DARSIVECAS LNTVTENCTP
LLPIYSTSTG NPYLANNATE TFECVISELL RKQICWDNVI NGIRERINYS GASAAAVDHF
GNSASLHDLE VALKSVLHES QVTLTNILTM SCVPPPKEIS PRSTGLSKLA IVGMACRLPG
GATDTEKFWD ILVKGLDVSR KVPADRFDIE THYDPTGKQM NKSMTQYGCF IDEPGLFDAP
FFNMSPREAQ TTDPQMRLAL VTAYEALEQA GYVGNRTNST KLERIGTYYG QAADDYREVN
QGQEVSTYYI PGGCRAFGPG RINYFFKFAG PSYSIDTACS SGLAAIEVAC QGLWNGVIDT
AVAGGVNVLT NPDGFAGLCN GHFLTKGHNA CKTWDSTADG YCRADGIGSL VIKRLEDAEA
DNDNILGIIL GAGTNHSAEA VSITHPHAGH QAYLSRQVLR QAGVDPLDVS YVELHGTGTQ
AGDYEEMQGI LDVYAPLTKR RSADNPLHIG AVKANLGHGE SVAGTTALMK VLLMFREQAI
PPHIGIKGEI NPKIPKDLAK RNLHIPMNLE SWRRRSDKKR LAVVNNFGAA GGNTTMVLEE
APIRCIEEMD PRQTHVISVS AKTKNSLVGN IERLIAYLDS NPDTSLADLS YTTMARRYQH
SWRVAMAPST MKDLKKQLSA YLEKIDLVKP AGKSGPPTVA FTFTGQGASH KSMNLALYHD
VPSFRDYIQR LDAIAQGQGF PSFIPAIDGS HPQDHQHSAV VTQLALVCSE MAMAQYWFSL
GIKPDVVIGH SLGEYAAMHV AGVISASDTI FMVGRRAQLL QEKCKLGSHS MVAVRASLEE
IKQNTSSTDS DAEFTIACIN GPTDTVLSGT KNAIDAVSKT LEQAGFRCTK LDVAFAFHSD
QTDPILDEFE DIVKASVSFQ EPKMPVISPL LGKVVFDGKT LNANYVRRAT RETVDFISAL
HNAQKMSTIS EDTVWIEVGP HAVCTNMIKK ILPATKLALP SMRRDADNWK TVSDSLAALH
SSGVEIFWNE FHRPFERRLR LLDLPTYSWN NQTYWLQYQG DWCLTKGNGF YGTLGQGSGS
AASSSSPSLL ASSVSNLHTS TVQCIIEETI DGTNGTVVMQ SDLMQPDLYT AAEGHRMNDC
AVVTSSIHAD IAFTLAEYML PKLLPASKKL KAIIQDLVVT KGLVANHDRN SPQLFRVTAT
TTDILHHGLD LTWQNVDNDG TVHEPFATAK ITFGDPEQWL SSWSPMVHLV QSRVEALEAL
VADGTANRFS RAMAYGLFAK NLVDYSEKYR GMQSVIMHGL EGFANVRLTD KESGNWTVPP
HFIDSVAHLA GFIMNCSDAI NTVDNYCVTP GWKAMQFAKP LTPGARYQSY VKMIPQADNS
GTYLGDVYIM QDGDIIGKVW GIEFRRYPRL LLSRFFSAPG KSSTTTTTKA SVSAPVKSKP
VETKLSAASK PPTVAQTGIP PEQKPAPEVQ PVTTNSPATA AAAPASTQAA DTDTVSAKAL
RLIANEAALD LSQLEDDAGF AELGIDSLMS LVIAEKFKIE LDVKVGGSLF LDYPTIGDLR
KWLEEYYS
//
