PFMAE_PESFW
ID PFMAE_PESFW Reviewed; 2155 AA.
AC W3X7U2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Conidial pigment polyketide synthase PfmaE {ECO:0000303|PubMed:28517364};
DE EC=2.3.1.- {ECO:0000305|PubMed:28517364};
DE AltName: Full=Conidial pigment biosynthesis cluster protein E {ECO:0000303|PubMed:28517364};
GN Name=PfmaE {ECO:0000303|PubMed:28517364}; ORFNames=PFICI_07101;
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140;
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX PubMed=28517364; DOI=10.1111/mmi.13711;
RA Zhang P., Wang X., Fan A., Zheng Y., Liu X., Wang S., Zou H., Oakley B.R.,
RA Keller N.P., Yin W.B.;
RT "A cryptic pigment biosynthetic pathway uncovered by heterologous
RT expression is essential for conidial development in Pestalotiopsis fici.";
RL Mol. Microbiol. 105:469-483(2017).
RN [3]
RP INDUCTION, AND FUNCTION.
RX PubMed=31116900; DOI=10.1111/mmi.14281;
RA Zhang P., Zhou S., Wang G., An Z., Liu X., Li K., Yin W.B.;
RT "Two transcription factors cooperatively regulate DHN melanin biosynthesis
RT and development in Pestalotiopsis fici.";
RL Mol. Microbiol. 112:649-666(2019).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a
CC bluish-green pigment forming a dark layer in the conidial wall that
CC protects the conidia from UV radiations (PubMed:28517364). The first
CC step of the pathway is the production of the pentaketide 1,3,6,8-
CC tetrahydroxynaphthalene (1,3,6,8-THN or T4HN) by the polyketide
CC synthase PfmaE though condensation of acetyl-CoA with malonyl-CoA. T4HN
CC is not stable and easily oxidizes into the stable form flaviolin
CC (PubMed:28517364). T4HN is also substrate of the hydroxynaphthalene
CC reductase PfmaG to yield scytalone (PubMed:28517364). The scytalone
CC dehydratase PfmaJ then reduces scytalone to 1,3,8-THN
CC (PubMed:31116900). 1,3,8-THN is then substrate of the
CC hydroxynaphthalene reductase PfmaI to yield vermelone (Probable).
CC Vermelone is further converted by the multicopper oxidase PfmaD to 1,8-
CC DHN (Probable). Finally the laccase PFICI_06862 transforms 1,8-DHN to
CC DHN-melanin (Probable). The roles of the 5-oxoprolinase PfmaA and the
CC proline iminopeptidase PfmaB within the cluster have not been
CC elucidated yet (Probable). {ECO:0000269|PubMed:28517364,
CC ECO:0000269|PubMed:31116900, ECO:0000305|PubMed:28517364,
CC ECO:0000305|PubMed:31116900}.
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000269|PubMed:28517364}.
CC -!- INDUCTION: Expression is positively regulazed by the cluster-specific
CC transcription factor pfmaF. {ECO:0000269|PubMed:28517364,
CC ECO:0000269|PubMed:31116900}.
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; a thioesterase (TE) domain that releases
CC the newly synthesized peptide from the enzyme; and 2 acyl-carrier
CC protein (ACP) that serve as the tethers of the growing and completed
CC polyketide via its phosphopantetheinyl arm.
CC {ECO:0000250|UniProtKB:Q5B0D0, ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased pigmentation, the lack of the
CC black pigment cell wall layer, but also incomplete multicellular
CC formation (PubMed:28517364). Abolishes the production of scytalone
CC (PubMed:28517364). Significantly reduces the germination rates under UV
CC treatment (PubMed:28517364). {ECO:0000269|PubMed:28517364}.
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DR EMBL; KI912112; ETS82099.1; -; Genomic_DNA.
DR RefSeq; XP_007833873.1; XM_007835682.1.
DR AlphaFoldDB; W3X7U2; -.
DR SMR; W3X7U2; -.
DR STRING; 1229662.W3X7U2; -.
DR EnsemblFungi; ETS82099; ETS82099; PFICI_07101.
DR GeneID; 19272114; -.
DR KEGG; pfy:PFICI_07101; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OMA; YWLDYHN; -.
DR OrthoDB; 68112at2759; -.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
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; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF53474; SSF53474; 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; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Melanin biosynthesis; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..2155
FT /note="Conidial pigment polyketide synthase PfmaE"
FT /id="PRO_0000445352"
FT DOMAIN 1653..1730
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1779..1856
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 8..245
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 381..755
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 910..1231
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1293..1608
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1738..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1911..2041
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 1740..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1760..1774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 553
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1001
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1690
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1816
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2155 AA; 233253 MW; 9F4BA1884908CE2E CRC64;
MAEQMSYLLF GDQSLDTHGF LADFYRQGNP SILAKTFLQR AGDSLRDEID RLPRCQRDRI
PQFRTLQQLN ERYHQQTIKF PGIDSALLCI TQLAHYIDRS EKEHQDVTAA ENTYLSGLCT
GLFAATAIAS SPSLSSLLPI AVQVSLMAYR VGSHVASLAE RLSPSDERSE SWTYVVPGAK
ETDAKPILAE FHETEGISPA AQAYVSAVSA SNIAISGPPA TLKSLFSKDL FESRPTAIPV
YGPYHAPHLH AAANLDKILR LDDEAVTAAF DGSKPRSHIV SCVTGQSFPE TDTKSLLKAV
VHEILNEPLL FHKALKGSLN SAKEFKGSRV LVIPYGPTQA ASTLANLLKA QTKLEVVLRT
PPQVSRESNG ASIGNHGSSG KCKLAIVGMA GRFPDAASHE KLWELLEKGI DAHRVVPADR
FPVETHVDPT GKAINTSHTP YGCWIENPGL FDPRFFNMSP REAFQTDPMQ RMALTTAYEA
LEMSGYVPNR TPSTRLDRIG TFYGQTSDDW REINAAQEVD TYYITGGVRA FGPGRINYHF
GFSGPSLNID TACSSSAAAL QVACTSLWAK ECDTAIVGGL SCMTNSDIFA GLSRGQFLSK
KGNCNTFDND ADGYCRADAC ASVIVKRLDD ALADKDNILA VVLGTSTNHS ADAISITHPH
GPTQSVLSRA ILDEAGVDPL DVDYVEMHGT GTQAGDGTEM VSVTDVFAPA NRHRASDRPL
YLGAIKSNVG HGEAASGITA LSKVLLMMKK NSIPPHVGIK GEINKTFPKD LGARGVNIAF
HKTPFQRKDG KPRRIFVNNF SAAGGNTGLL LEDGPRYKTA EADPRSVHVV TVTAKSKSAM
IRNAEGLVQW MEQNPSTPVS DVAYTTTARK IQHYWRMNVA AGSLPEAIQA IKERLKSTFV
PVSPEQPKVA FMFTGQGSHY AGLGKELYAH YAIFRDAIDE YDQLAGIHGF PSFLPLIDGS
EPDVQNLSPV VVQLGLCSFE MALARLWQSW GIQPGAVLGH SLGEYAALHV AGVLSASDTI
YLVGARAQLL VNKCTAGTHA MLAVQGSVET VKEALGARAE STNVACINGP RETVLSGASS
EVAEIAEQLG GAGFKCTQLK VPFAFHSAQV EPILDDFESL ARSVRFETPK VPVISPLLGK
LVDNEPINPA YLRNHAREAV NFLGGLVSAQ QSGMIDEKTV WLEVGPHPVC ANMVKAAFGA
TTIAVPTLRR NEATYKTLSS SLCTLHSAGL NLDWNEFHRD FDASVRLLDL PSYAFDYKNY
WLQYTGDWSL TKNRGALPAS TKAIEAPKPK LSTTTVQKVV REEVKGDIAI LETESEMTRD
DLRLVCSGHM VNGTALTPSS LYGDMAITAC EYAYKLLRPD AKNIGCNVSH MEVPKTLIFN
GKAKSQVLRM SVKANAAEGF ADLSWTSGEG AQKTEHANCK VFFGDNEEWL GEFERVNYLI
KSRIDALRAA EQRGDASKIG RGLAYKLFAA LVDYDRRYRG MESVILDSET CEATAKVVFQ
TSPEDGTFHT APYWIDSVCH ISGFILNGSD AIDSREQVFI SHGWGSMRFA ERLSAEKTYQ
TYIRMQNVKG SKMMSGDAYI FDGDKLIGIA GDVRFQAIPR KVLNVVLPPQ GAAAAGSAPA
RAPAAAAKPA AKAAPKEKKQ VTSANLPAVN KSLTKNSVVA QVMEIIAKET GVSHDELADN
IAFSDLGVDS LMGLTISGRL REELELNVDS HAFNDHATVG AFKAFLAQFE SADAAMVEEN
AHSSASSDSA DMETESNFTT PSDDSEKDEV KGDAPAADGN VSELQDIVRS TISAEMGVEV
EEVIAAPDLA ALGMDSLMSL SILGILREKT GLNIPSDLLG HNPSLKDIEK ALGIEDKPKR
AAPKSAKQEP AKPEPKVQGE AKAHTNPVDN YPHRKATSVL LQGNHRTAKK QLFMIPDGSG
SATSYTEISE VGSDVAVWGL FSPFMKTPDE YNCGVYGMAT KFIQEMKRRQ PEGPYAVAGW
SAGGVIAYEI VNQLTKANEE VSNLLIIDAP CPITIEPLPA GLHAWFASIG LLGEGDDAEA
KKIPEWLLPH FAASVTALSN YDAEPIPADK CPKVTVIWCE DGVCKLPTDP RPDPYPTGHA
LFLLDNRSDF GPNRWDEYLD SKKMTFHHMP GNHFSMMHGP LAKQLGGFMR DGMKS
