STHB_PHANO
ID STHB_PHANO Reviewed; 315 AA.
AC Q0UK53;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=FAD-linked oxidoreductase sthB {ECO:0000303|PubMed:31553484};
DE EC=1.-.-.- {ECO:0000305|PubMed:31553484};
DE AltName: Full=FAD-dependent BBE enzyme-like protein {ECO:0000303|PubMed:31553484};
DE AltName: Full=Stemphyloxin II biosynthesis cluster protein B {ECO:0000303|PubMed:31553484};
GN Name=sthB {ECO:0000303|PubMed:31553484}; ORFNames=SNOG_07861;
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: FAD-linked oxidoreductase; part of the gene cluster that
CC 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=betaenone C = betaenone A; Xref=Rhea:RHEA:61896,
CC ChEBI:CHEBI:145053, ChEBI:CHEBI:145055;
CC Evidence={ECO:0000269|PubMed:31553484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61897;
CC Evidence={ECO:0000269|PubMed:31553484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=stemphyloxin I = stemphyloxin II; Xref=Rhea:RHEA:62716,
CC ChEBI:CHEBI:145066, ChEBI:CHEBI:145070;
CC Evidence={ECO:0000269|PubMed:31553484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62717;
CC Evidence={ECO:0000269|PubMed:31553484};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31553484}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; CH445335; EAT85327.2; -; Genomic_DNA.
DR RefSeq; XP_001798188.1; XM_001798136.1.
DR AlphaFoldDB; Q0UK53; -.
DR SMR; Q0UK53; -.
DR STRING; 13684.SNOT_07861; -.
DR EnsemblFungi; SNOT_07861; SNOT_07861; SNOG_07861.
DR GeneID; 5975081; -.
DR KEGG; pno:SNOG_07861; -.
DR eggNOG; ENOG502R8I5; Eukaryota.
DR HOGENOM; CLU_018354_4_2_1; -.
DR InParanoid; Q0UK53; -.
DR OrthoDB; 827142at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..315
FT /note="FAD-linked oxidoreductase sthB"
FT /id="PRO_0000448657"
FT DOMAIN 19..201
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 315 AA; 33144 MW; C276861EDED3E97C CRC64;
MMNPFFQNTS CSPYYRTDQP CSLGNYVSYA IPVAGVADIV AAINFTQTHN VRLVIKNTGH
DYMGKSTGRG ALSLWTHNLK SRQLVNYSSA HYTGPAIKVG AGVTGGEALV HASASGYRIV
SGDCPTVGYS GGYSSGGGHS ILNSVHGLAA DNVLEWEVVT ADGRHVVASP DQNSDLYWAM
SGGGGGTFAV ALSMTSRVHA DSIIGAASLS FNATSAPSND SFVSALNAWW AFLPSLVDVG
ATPSWNIFAG NFLVPNTTAP GRTAADMDTL YSPFLSELKR LGIPYAFESF SAPNYLQHYN
DTDGPLPDGP LAAWA
