ID   BFOE_ASPBC              Reviewed;         372 AA.
AC   A0A1L9URE0;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=O-methyltransferase bfoE {ECO:0000303|PubMed:31067027};
DE            EC=2.1.1.- {ECO:0000305|PubMed:31067027};
DE   AltName: Full=Bifonsecin B biosynthesis cluster protein E {ECO:0000303|PubMed:31067027};
GN   Name=bfoE {ECO:0000303|PubMed:31067027}; ORFNames=ASPBRDRAFT_438143;
OS   Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101740 / IMI 381727 / IBT 21946;
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=31067027; DOI=10.1021/acs.biochem.9b00291;
RA   Obermaier S., Mueller M.;
RT   "Biaryl-forming enzymes from Aspergilli exhibit substrate-dependent
RT   stereoselectivity.";
RL   Biochemistry 58:2589-2593(2019).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of bifonsecin B, a dimeric gamma-
CC       naphthopyrone (PubMed:31067027). The first step in the biosynthesis of
CC       bifonsecin B is the production of gamma-naphthopyrone precursor YWA1 by
CC       the non-reducing polyketide synthase albA, via condensation of one
CC       acetyl-CoA starter unit with 6 malonyl-CoA units (PubMed:31067027).
CC       YWA1 is then methylated by bfoE at position C-6 to yield foncesin which
CC       is further methylated at position C-8 by bfoD to produce fonsecin B
CC       (Probable). A key enzyme in the biosynthetic pathway is the cytochrome
CC       P450 monooxygenase bfoB which catalyzes the oxidative dimerization of
CC       fonsecin B to bifonsecin B (PubMed:31067027). Bfob also catalyzes the
CC       oxidative dimerization of rubrofusarin B into nigerone
CC       (PubMed:31067027). The stereoselectivity of bfoB is influenced by the
CC       two natural monomeric substrates; homodimerization of fonsecin B yields
CC       a stereochemically pure biaryl, M-foncerine B, while rubrofusarin B
CC       yields a mixture of enantiomers M- and P-nigerone (PubMed:31067027).
CC       {ECO:0000269|PubMed:31067027, ECO:0000305|PubMed:31067027}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:31067027}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; KV878681; OJJ74126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9URE0; -.
DR   SMR; A0A1L9URE0; -.
DR   EnsemblFungi; OJJ74126; OJJ74126; ASPBRDRAFT_438143.
DR   VEuPathDB; FungiDB:ASPBRDRAFT_438143; -.
DR   OrthoDB; 817726at2759; -.
DR   Proteomes; UP000184499; Unassembled WGS sequence.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..372
FT                   /note="O-methyltransferase bfoE"
FT                   /id="PRO_0000448927"
FT   ACT_SITE        285
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   372 AA;  41342 MW;  648A5D643294E04F CRC64;
     MTAAQNAPIP EAGKKVMSTV TLAPALGFVP VAVHFDLFGC LQEIGKPATA QDVCNIHRTR
     YGDTNLSVSL ANDTLFLMGG LGFLDLLPDD VYQANDVTRY LVDTPSAQHG AMHFTSEGLL
     ASAFLMRRLM DTNFEYPFQE CDTPFQYAYK LMGNDSLARE HVYSVMHHTG RLDSFNTFMT
     GKFGRWGTMP DRVRKLGYDL DGLMQSTAPE KLRIVDIGGG RGELLLEMQA AYPHLLQKEN
     LVLQEYNADI GVVPKVTEMA WNYKEDASEQ PVKGALLYSM AHVLHNLSDI ESIKLLAKVA
     RVMAPTSRLL IQEFTKNAAS STTHAAMILM HAGRERTRAE WRDLAAFAGL EITFEAYPPN
     GECLVEMRKV LN