STHF_PHANO
ID STHF_PHANO Reviewed; 513 AA.
AC Q0UK49;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Cytochrome P450 monooxygenase sthF {ECO:0000303|PubMed:31553484};
DE EC=1.-.-.- {ECO:0000305|PubMed:31553484};
DE AltName: Full=Stemphyloxin II biosynthesis cluster protein F {ECO:0000303|PubMed:31553484};
GN Name=sthF {ECO:0000303|PubMed:31553484};
GN ORFNames=SNOG_07865 {ECO:0000312|EMBL:EAT85331.1};
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: Cytochrome P450 monooxygenase; 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=dehydroprobetaenone I + H(+) + NADPH + O2 = epoxybetaenone +
CC H2O + NADP(+); Xref=Rhea:RHEA:61860, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:145061, ChEBI:CHEBI:145069;
CC Evidence={ECO:0000269|PubMed:31553484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61861;
CC Evidence={ECO:0000269|PubMed:31553484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dehydroprobetaenone I + 3 H(+) + 3 NADPH + 3 O2 = betaenone C
CC + 3 H2O + 3 NADP(+); Xref=Rhea:RHEA:61856, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:145053, ChEBI:CHEBI:145061;
CC Evidence={ECO:0000269|PubMed:31553484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61857;
CC Evidence={ECO:0000269|PubMed:31553484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H(+) + 3 NADPH + 3 O2 + probetaenone I = betaenone B + 3 H2O
CC + 3 NADP(+); Xref=Rhea:RHEA:62720, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:145054, ChEBI:CHEBI:145062;
CC Evidence={ECO:0000269|PubMed:31553484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62721;
CC Evidence={ECO:0000269|PubMed:31553484};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31553484}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CH445335; EAT85331.1; -; Genomic_DNA.
DR RefSeq; XP_001798192.1; XM_001798140.1.
DR AlphaFoldDB; Q0UK49; -.
DR SMR; Q0UK49; -.
DR EnsemblFungi; SNOT_07865; SNOT_07865; SNOG_07865.
DR GeneID; 5975085; -.
DR KEGG; pno:SNOG_07865; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_11_1; -.
DR InParanoid; Q0UK49; -.
DR OMA; NIYVTHI; -.
DR OrthoDB; 1247045at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Cytochrome P450 monooxygenase sthF"
FT /id="PRO_0000448652"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 452
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 513 AA; 59257 MW; DE864BD9B66B8653 CRC64;
MGLQFLAPGE KVFPSLHRII ISTFALIAAY IFIVRPLRNI LFHPLKKYPG PKLFGASSIP
YGFYYMTGKW HLKIRNLHAT YGPIVRIGPD ELSYACPEAW EDIYGRYVPT KRRENPKPVW
YCSPDAHDMV GASLGDHGRM RRVMAPGFTY SAMCKQEPLI KGHVDMFLSK LCSLCGDGRA
EVNILDWLTY CTFDLIGDLS FGEPFGCMEN NMLHPWLQLV FANIYITHII LLCQRIPFFY
LFLPIKTTYQ LWRDFRRHVV LLREVVERRL SLSTPRDDFL DVMTTKQTST LYMTKEEIFK
NAILLTGGGA ETTSSSLSGM MYMLTMRPDV KEKILEELRD TFPSEDDINM RSVAQLTYTG
AFIEESMRYY PPGPNTMWRI TPPAGNTILG DYIPGNTIVG IPHRVLYRSE AYWKDADGFR
PERWLPDSQR PAEFDEDKRE GFHPFSYGPR ACIAMNLAYA EMRYILARFL WHFDIEATKE
SKKWMDDQKA YLVWDKPGLF VHLKPRAGVK VAA
