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PIG15_CLAP2
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   25-MAY-2022, entry version 49.
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}.
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DR   EMBL; CAGA01000032; CCE31584.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1WG96; -.
DR   SMR; M1WG96; -.
DR   STRING; 1111077.M1WG96; -.
DR   EnsemblFungi; CCE31584; CCE31584; CPUR_05437.
DR   VEuPathDB; FungiDB:CPUR_05437; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_6_1_1; -.
DR   OrthoDB; 68112at2759; -.
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   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.40.366.10; -; 2.
DR   Gene3D; 3.40.47.10; -; 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; IPR020807; PKS_dehydratase.
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   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; PF14765; PS-DH; 1.
DR   Pfam; PF16073; SAT; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 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          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          409..843
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          941..1265
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1375..1650
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
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
 
 
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