DESS_ASPDE
ID DESS_ASPDE Reviewed; 1733 AA.
AC A0A0N9HNS9;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Desertorin synthase {ECO:0000303|PubMed:26389790};
DE EC=2.3.1.- {ECO:0000305|PubMed:26389790};
DE AltName: Full=Desertorin biosynthesis cluster protein S {ECO:0000303|PubMed:26389790};
DE AltName: Full=Non-reducing polyketide synthase desS {ECO:0000303|PubMed:26389790};
GN Name=desS {ECO:0000303|PubMed:26389790};
GN ORFNames=EMD_0002 {ECO:0000303|PubMed:26389790};
OS Aspergillus desertorum (Emericella desertorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810909;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=CBS 653.73 / NBRC 30840;
RX PubMed=26389790; DOI=10.1021/jacs.5b06776;
RA Mazzaferro L.S., Huettel W., Fries A., Mueller M.;
RT "Cytochrome P450-catalyzed regio- and stereoselective phenol coupling of
RT fungal natural products.";
RL J. Am. Chem. Soc. 137:12289-12295(2015).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of the bicoumarin desertorin
CC (PubMed:26389790). The non-reducing polyketide synthase desS first
CC catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-
CC methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A
CC molecules (PubMed:26389790). Further O-methylation by desB leads to the
CC formation of 7-demethylsiderin (PubMed:26389790). Then, an oxidative
CC phenol coupling catalyzed by the cytochrome P450 monooxygenase desC
CC forms the 6,8'-dimer M-desertorin A via dimerization the monomeric
CC precursor, 7-demethylsiderin (PubMed:26389790). M-desertorin A is
CC further converted to M-desertorin C (PubMed:26389790).
CC {ECO:0000269|PubMed:26389790}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26389790}.
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}.
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DR EMBL; KT583602; ALG03237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N9HNS9; -.
DR SMR; A0A0N9HNS9; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; 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; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..1733
FT /note="Desertorin synthase"
FT /id="PRO_0000442164"
FT DOMAIN 1659..1733
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 21..358
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 375..802
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 406..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..1211
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1299..1594
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1608..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1696
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1733 AA; 189633 MW; 47BC736083EE0CD1 CRC64;
MKVLFFSNKF PVEEHADLFQ RIRQQSRSSR HAVLRQLLDE CTAAVREEIR LLPAEIRTRL
PPFQSILDLA EGFRWERSPL AGTFECVFLC LAELCLFVGD YEARPQAFKF TRSDSVFTGL
GLGFLAATAI VASPTLIDVP ATAADVIRIA MRAGLVVYHQ GQNLEPQSLS APLQSWTTLV
KRLGEEAVQR ELDCFNSAIP RPSQIYISVV EPDGSVFING PPSIMRLLFS TPGPLQSAPR
APLPVYGGPC HAAHLYDRSH VSWIVKHVRS EIAWREFSDA APLLSMADGQ PLRAQTALEL
FESAAYVLLT GIIRWGNVLA ALEEREDGAI QIESCGHSTP VEKLMRVLHA PTRDLTEWLS
DEIEAVPGTH ADCRIAVVGM SCRLPGADDL EHFWELLEQG RDVHQHVPPD RYDVQSHTDP
TGRRMNTSQT PFGCFIDSPG LFDAGFFDMS PREAGQTDPT HRLALLTAYE ALQQSGYIPD
RTLSTIRETV ATIYGQCSDD YREANAGQEI DMYFIPGNYR AFAPGRISYF FKFSGPSFSC
DTACSASLAA VQIACATLSR GEANMVVAGG LNILTSSDSF AGLSRAHFLS KTGGCKVFDD
GADGYCRADG VGSLVLKRLA DAQRDNDNIL GVILAAATNH SSAAVSITHP HAPTQEELYR
NVLRQAGVSP LDVDLVEMHG TGTQAGDAAE IESVTRVFSP SRRSERLYIG SVKANLGHGE
AAAGVTALIK ALLIFQHNAI PKHVGIKTAL NSRFPDLGQL NVHIPGETVP WSPRPNRKRY
VMVNNFSAAG GNTALLLEEP PQRPTPGPAC AQTRFVVTVS AKNPLSLRRN LERLMAFLRQ
HQPPVHLGSL AYTTTARRIH YPHRIAVQGA SIADIIKHLE LRLADLSLAH PQGAVARPPP
IAFVFSGQGS FYPGISHDLL EHYPPYAREI HQLDALCLRH GFPSILPALT SSENSPSPLV
TQLTTVCVQI ALTHLWKSLA ITPAVVIGAS LGEYAALHAT GALSASDTIF LVGQRGLLMQ
DLCTANTHTM LAVQATANEI AGCVPDSLSY EVACINSHRS ITIAGTRSNI TAIKASLESR
GYRATELNVP YAFHSSHMDP ILEKFNAIAQ QATARALKVP LISPLLVDVL HEHTTLPASY
LAEATRGRVR FSEALEKAHQ ATLITDQTVF VEIGIHPTYS NAVRSTVHNI AAVVPTLRSD
QDNWHTLAGS MAALYEAAAG LDWNAWFEPF EPELRLLDLP RYAWNLKNHW IQHNGDWLLW
KDKDRDRDNG KCMTHPDDGR GLYTPLLHRI VEETFWAGGG RVVMESNVHQ EEFFAVASGH
KMCGRPVVSV FSYPDMALSL ARFVYTKVHP DISPPAMDFG NVHIFEGLIP HKDRSSPQWV
RLQIKTTSVK HQLQVSFHRV GEDRVDQLAT GTVSVGNAAS WLSEWSGIAH LVSSRIKALQ
DLVHEGRADR LTRDTVYHLF RNSIVDYSPA YRGIQSAVID GLEAVADVVL ASSNMDRWTA
PPHHVDSIAH VCGFVLNAGN AADHDNINTV YVMEGWRSMR FAKPLVSGRL YRSYVRMVPA
RDTGFFSGDV YVLDVAEDEV TGLLAGVTLR PLPRILMHRF FDPADDAHNW GNSPAKPEAK
PEMVPTSGSS SAAGSPSGSS AGPLSIPERL ADPSETSFQS KASKVSKALA LIASETGIDM
QDLNDETCLA QIGVDSLLSL VLVEKFALEL GVHFPGSFFL DFPTVGEVKR QML
