STHC_PHANO
ID STHC_PHANO Reviewed; 314 AA.
AC Q0UK52;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Short-chain dehydrogenase/reductase sthC {ECO:0000303|PubMed:31553484};
DE EC=1.1.1.- {ECO:0000305|PubMed:31553484};
DE AltName: Full=Stemphyloxin II biosynthesis cluster protein C {ECO:0000303|PubMed:31553484};
GN Name=sthC {ECO:0000303|PubMed:31553484}; ORFNames=SNOG_07862;
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: Short-chain dehydrogenase/reductase; part of the gene cluster
CC that mediates the biosynthesis of the phytotoxin stemphyloxin II
CC (PubMed:31553484). The first step of the pathway is the synthesis of
CC dehydroprobetaenone I by the polyketide synthase sthA and the enoyl
CC reductase sthE via condensation of one acetyl-CoA starter unit with 7
CC malonyl-CoA units and 5 methylations (PubMed:31553484). The C-terminal
CC reductase (R) domain of sthA catalyzes the reductive release of the
CC polyketide chain (PubMed:31553484). Because sthA lacks a designated
CC enoylreductase (ER) domain, the required activity is provided the enoyl
CC reductase sthE (PubMed:31553484). The short-chain
CC dehydrogenase/reductase sthC then catalyzes reduction of
CC dehydroprobetaenone I to probetaenone I (PubMed:31553484). The
CC cytochrome P450 monooxygenase sthF catalyzes successive epoxidation,
CC oxidation (resulting from epoxide opening) and hydroxylation to install
CC a tertiary alcohol in the decaline ring to yield betaenone C from
CC dehydroprobetaenone I and betaenone B from probetaenone I
CC (PubMed:31553484). The FAD-linked oxidoreductase sthB is responsible
CC for the conversion of betaenone C to betaenone A via an intramolecular
CC aldol reaction between C-1 and C-17 to form the bridged tricyclic
CC system in betaenone A (PubMed:31553484). Finally, the cytochrome P450
CC monooxygenase sthD catalyzes the hydroxylation of C-15 to afford the
CC final metabolite stemphyloxin II (PubMed:31553484).
CC {ECO:0000269|PubMed:31553484}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + dehydroprobetaenone I = A + probetaenone I;
CC Xref=Rhea:RHEA:61864, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:145061, ChEBI:CHEBI:145062;
CC Evidence={ECO:0000269|PubMed:31553484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61865;
CC Evidence={ECO:0000269|PubMed:31553484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + betaenone C = A + betaenone B; Xref=Rhea:RHEA:61900,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:145053,
CC ChEBI:CHEBI:145054; Evidence={ECO:0000269|PubMed:31553484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61901;
CC Evidence={ECO:0000269|PubMed:31553484};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31553484}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CH445335; EAT85328.2; -; Genomic_DNA.
DR RefSeq; XP_001798189.1; XM_001798137.1.
DR AlphaFoldDB; Q0UK52; -.
DR SMR; Q0UK52; -.
DR STRING; 13684.SNOT_07862; -.
DR EnsemblFungi; SNOT_07862; SNOT_07862; SNOG_07862.
DR GeneID; 5975082; -.
DR KEGG; pno:SNOG_07862; -.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_6_1; -.
DR InParanoid; Q0UK52; -.
DR OrthoDB; 1032903at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..314
FT /note="Short-chain dehydrogenase/reductase sthC"
FT /id="PRO_0000448655"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 48..56
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 75..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 111..113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 222..226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 255..257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 314 AA; 34055 MW; 008CEAD9347C4FDF CRC64;
MAPAETTGNV QRPEAGKQSM GSFWTQMFPP KPTYTEEQVP DLTGKIFIVT GSSSGVGKEA
ARMLYAKNAK VYMAARPGPK LPAAINSVQE AVPKSGGALI PLELDLADLA VVKKAVEKFT
SLETKLHGLI NNAAVQALKD TDGDARTAQG HEIHMGVNVL APFLFTRLLT GVLTATARQE
PPGTVRVVWV SSMGTETIGE KRRGLSPDYV DYWPLMSPLE RYGLSKAGNW LHGVEFARRY
AADGIASFPI NPGHLKSDLY REGGALFKFA LKPVLYPPTY GAYVELFAAL SPTLTLKDSG
AWSKYVEMVY FPDC
