STHE_PHANO
ID STHE_PHANO Reviewed; 364 AA.
AC Q0UK50;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Trans-enoyl reductase sthE {ECO:0000303|PubMed:31553484};
DE EC=1.-.-.- {ECO:0000305|PubMed:31553484};
DE AltName: Full=Stemphyloxin II biosynthesis cluster protein E {ECO:0000303|PubMed:31553484};
GN Name=sthE {ECO:0000303|PubMed:31553484}; ORFNames=SNOG_07864;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=31553484; DOI=10.1002/chem.201904360;
RA Li H., Hu J., Wei H., Solomon P.S., Stubbs K.A., Chooi Y.H.;
RT "Biosynthesis of a Tricyclo[6.2.2.02,7]dodecane System by a Berberine
RT Bridge Enzyme-like Intramolecular Aldolase.";
RL Chemistry 25:15062-15066(2019).
CC -!- FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates
CC the biosynthesis of the phytotoxin stemphyloxin II (PubMed:31553484).
CC The first step of the pathway is the synthesis of dehydroprobetaenone I
CC by the polyketide synthase sthA and the enoyl reductase sthE via
CC condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units
CC and 5 methylations (PubMed:31553484). The C-terminal reductase (R)
CC domain of sthA catalyzes the reductive release of the polyketide chain
CC (PubMed:31553484). Because sthA lacks a designated enoylreductase (ER)
CC domain, the required activity is provided the enoyl reductase sthE
CC (PubMed:31553484). The short-chain dehydrogenase/reductase sthC then
CC catalyzes reduction of dehydroprobetaenone I to probetaenone I
CC (PubMed:31553484). The cytochrome P450 monooxygenase sthF catalyzes
CC successive epoxidation, oxidation (resulting from epoxide opening) and
CC hydroxylation to install a tertiary alcohol in the decaline ring to
CC yield betaenone C from dehydroprobetaenone I and betaenone B from
CC probetaenone I (PubMed:31553484). The FAD-linked oxidoreductase sthB is
CC responsible for the conversion of betaenone C to betaenone A via an
CC intramolecular aldol reaction between C-1 and C-17 to form the bridged
CC tricyclic system in betaenone A (PubMed:31553484). Finally, the
CC cytochrome P450 monooxygenase sthD catalyzes the hydroxylation of C-15
CC to afford the final metabolite stemphyloxin II (PubMed:31553484).
CC {ECO:0000269|PubMed:31553484}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 10 AH2 + 2 H(+) + 7 malonyl-CoA + 5 S-adenosyl-L-
CC methionine = 10 A + 7 CO2 + 8 CoA + dehydroprobetaenone I + 6 H2O + 5
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51348, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:145061; Evidence={ECO:0000269|PubMed:31553484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51349;
CC Evidence={ECO:0000269|PubMed:31553484};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31553484}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; CH445335; EAT85330.1; -; Genomic_DNA.
DR RefSeq; XP_001798191.1; XM_001798139.1.
DR AlphaFoldDB; Q0UK50; -.
DR SMR; Q0UK50; -.
DR EnsemblFungi; SNOT_07864; SNOT_07864; SNOG_07864.
DR GeneID; 5975084; -.
DR KEGG; pno:SNOG_07864; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_16_1_1; -.
DR InParanoid; Q0UK50; -.
DR OMA; TGTMACQ; -.
DR OrthoDB; 727365at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..364
FT /note="Trans-enoyl reductase sthE"
FT /id="PRO_0000448653"
FT BINDING 51..54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 137..144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 172..175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 195..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 261..262
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 281..285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 351..352
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 364 AA; 38355 MW; 7F0DEE6D931BC913 CRC64;
MLPANGQTAV IQSKTSSHGL PLVVAHGRPL PPLPTPYHVR VRVLAVGLNP TDYKMVTHFF
MQDNTAGCDF CGIVEEAGPQ SVLGLGLRVC GADFPYRPSN PYNGAFAEYA TADSRHLLRI
PDGVSDLQAA GIGAIGWGTA ALAISDPAAL DLPGLPSRPD SRGLPVLVYG GATATGIMAI
QMLKLSGYSP IAVCSESSAP LCMSLGAIGT ASYTSVTCAE DIKAIAKGSK IKHALDCITD
VESMAICLAS LSRTGGRYAC LEAFPDAWLT RRAIAVKVVM GFEGQNVDVD LGHPVYTRKA
NPALHAVAGE WARELQLLLN DGQIKTQPMQ EIGGSFEGVI KALEMLQRGD VKGKKLAIRI
AYSK
