SDNS_SORAA
ID SDNS_SORAA Reviewed; 772 AA.
AC A0A1B4XBH9;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Transcription factor sdnS {ECO:0000303|PubMed:27072286};
DE AltName: Full=Sordarin/hypoxysordarin biosynthesis cluster protein S {ECO:0000303|PubMed:27072286};
GN Name=sdnS {ECO:0000303|PubMed:27072286};
OS Sordaria araneosa (Pleurage araneosa).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=573841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 36386 / NRRL 3196;
RX PubMed=27072286; DOI=10.1038/ja.2016.40;
RA Kudo F., Matsuura Y., Hayashi T., Fukushima M., Eguchi T.;
RT "Genome mining of the sordarin biosynthetic gene cluster from Sordaria
RT araneosa Cain ATCC 36386: characterization of cycloaraneosene synthase and
RT GDP-6-deoxyaltrose transferase.";
RL J. Antibiot. 69:541-548(2016).
CC -!- FUNCTION: Transcription factor; part of the gene cluster that mediates
CC the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics
CC with a unique tetracyclic diterpene aglycone structure
CC (PubMed:27072286). First, the geranylgeranyl diphosphate synthase sdnC
CC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate
CC (PubMed:27072286). The diterpene cyclase sdnA then catalyzes the
CC cyclization of GGDP to afford cycloaraneosene (PubMed:27072286).
CC Cycloaraneosene is then hydroxylated four times by the putative
CC cytochrome P450 monooxygenases sdnB, sdnE, sdnF and sdnH to give a
CC hydroxylated cycloaraneosene derivative such as cycloaraneosene-
CC 8,9,13,19-tetraol (PubMed:27072286). Although the order of the
CC hydroxylations is unclear, at least C8, C9 and C13 of the
CC cycloaraneosene skeleton are hydroxylated before the sordaricin
CC formation (PubMed:27072286). Dehydration of the 13-hydroxy group of the
CC hydroxylated cycloaraneosene derivative might be catalyzed by an
CC unassigned hypothetical protein such as sdnG and sdnP to construct the
CC cyclopentadiene moiety (PubMed:27072286). The FAD-dependent
CC oxidoreductase sdnN is proposed to catalyze the oxidation at C9 of the
CC hydroxylated cycloaraneosene derivative and also catalyze the Baeyer-
CC Villiger oxidation to give the lactone intermediate (PubMed:27072286).
CC The presumed lactone intermediate would be hydrolyzed to give an
CC acrolein moiety and a carboxylate moiety (PubMed:27072286). Then,
CC [4+2]cycloaddition would occur between the acrolein moiety and the
CC cyclopentadiene moiety to give sordaricin (PubMed:27072286). SdnN might
CC also be involved in the [4+2]cycloaddition after the hypothesized
CC oxidation to accommodate the oxidized product and prompt the
CC [4+2]cycloaddition (PubMed:27072286). GDP-6-deoxy-D-altrose may be
CC biosynthesized from GDP-D-mannose by the putative GDP-mannose-4,6-
CC dehydratase sdnI and the short-chain dehydrogenase sdnK
CC (PubMed:27072286). The glycosyltransferase sdnJ catalyzes the
CC attachment of 6-deoxy-D-altrose onto the 19-hydroxy group of sordaricin
CC to give 4'-O-demethylsordarin (PubMed:27072286). The methyltransferase
CC sdnD would complete the biosynthesis of sordarin (PubMed:27072286).
CC Sordarin can be further modified into hypoxysordarin (PubMed:27072286).
CC The unique acyl chain at the 3'-hydroxy group of hypoxysordarin would
CC be constructed by an iterative type I PKS sdnO and the trans-acting
CC polyketide methyltransferase sdnL. SdnL would be responsible for the
CC introduction of an alpha-methyl group of the polyketide chain
CC (PubMed:27072286). Alternatively, the beta-lactamase-like protein sdnR
CC might be responsible for the cleavage and transfer of the polyketide
CC chain from the PKS sdnO to sordarin (PubMed:27072286). Two putative
CC cytochrome P450 monooxygenases, sdnQ and sdnT, might catalyze the
CC epoxidations of the polyketide chain to complete the biosynthesis of
CC hypoxysordarin (PubMed:27072286). Transcriptional regulators sdnM and
CC sdnS are presumably encoded for the transcriptional regulation of the
CC expression of the sdn gene cluster (PubMed:27072286).
CC {ECO:0000269|PubMed:27072286}.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:27072286}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR EMBL; LC079035; BAV32163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B4XBH9; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; DNA-binding; Metal-binding; Nucleus;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..772
FT /note="Transcription factor sdnS"
FT /id="PRO_0000441066"
FT DNA_BIND 23..53
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 94..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 85413 MW; 615554BA744325C3 CRC64;
MTEQAQREAE LKRRKVRKGT HSCWECRRRK IRCQFGAGND TVCLPCQARG STCRSQEYVD
KDARPSQQPD RRMAQRLGRL EELMARLVDR ILPEAGGQLA NRSTTQSNRG SRSPSPDSAQ
NEGLAFHQTL DVLEASLGPN TPAGLLLGLR DAAQPASMLT PESDHSPAPS KLTPSRNSKT
SRSLYALFPP QEALPVLMKA NAGPYYLTSL FSSFRDLIEG KVETANSVTV IPPAVSHPTV
LARRLLQICI CMQQLNPGYD TSPLQIKGTI PEYMNNVVTT VTNLVTSIDE IVSTGEGLES
LVLLGLWHAN AGNLRKAWLT YRRALSLGQL MGIDRGSTRA LKFVDTNTDP QKHSTPAGLW
YRINACDRAS SLLLGLPAGD LDNSFATEEA MKRDTAMERL EKIHVVLTGR IIERNATRSS
SEAYAVTQSI DSELERAATS MGADWWSEPD FDVTDETGHK LGEMLRQMLQ MRHFDLLILL
HLPYMLRDPS ENRYDYSKTT CARSSREVLK RFIPFRSKVT AAWACRHVDY SALVASMTLL
VGYLRQHQHA TEPAPTCKER NEDRKLIEVV RERMQHVAIT NRDKVTQESA DILGQMMPIL
DLIDRSLMGD LSECNSHVLK CLHLKVPYLG TINFHPNVNV PEGQSANTPY SRRDNAGTIP
GPVSVAGAAT SGLEQLQPRM AGLSTAHDAA MPSVTAMSQG GDSMQVDMAT FDPALLPPDT
SIDGMYMDFD EQPQDGVHEI PDLMAGVEDW VLQGLDTTYW SLLNGNNMAW GG
