ID   BFOD_ASPBC              Reviewed;         424 AA.
AC   A0A1L9UR19;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=O-methyltransferase bfoD {ECO:0000303|PubMed:31067027};
DE            EC=2.1.1.- {ECO:0000305|PubMed:31067027};
DE   AltName: Full=Bifonsecin B biosynthesis cluster protein D {ECO:0000303|PubMed:31067027};
GN   Name=bfoD {ECO:0000303|PubMed:31067027}; ORFNames=ASPBRDRAFT_39215;
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; OJJ74127.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9UR19; -.
DR   SMR; A0A1L9UR19; -.
DR   STRING; 767769.A0A1L9UR19; -.
DR   EnsemblFungi; OJJ74127; OJJ74127; ASPBRDRAFT_39215.
DR   VEuPathDB; FungiDB:ASPBRDRAFT_39215; -.
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   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   SUPFAM; SSF46785; SSF46785; 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..424
FT                   /note="O-methyltransferase bfoD"
FT                   /id="PRO_0000448926"
FT   ACT_SITE        326
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         275
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   424 AA;  46912 MW;  95A6C19315175B63 CRC64;
     MADCLSSQLE RYANQVASSA GIIISHLKTL KDEPSTLPSE TTVPTAIGTA QLQLAEAAFQ
     LLHLTRDPGN VLTNLTVDLQ VISSVRWLLH FEIPSLVPQE GTISYQELSC LANVPDNLLR
     SHLRLAMTCH LFQESGPTGM VAHSAVSRKL ASDPSLAYWG QYFANTVFPT ATQSVNATAT
     WADSKQLNET AHNLAFDHRG TFFDYIAQDP ARTVEFANSM RAVSTTGPFD TCHLCKSFDW
     SSLGDGVVVD MGGSTGHASI TLAESFPSLR FVVQDLPDVV SDSIKRLEER QLPLSVTSRI
     RFQGHSLFHL QPVKGAAVYL LRQILHDWPN QEAIKILRSI VPAMGPKSRI FIADIVLPKT
     GSIPATEERV MRCNDLLLHQ FTNTLERTFE DWQAIVSRVD DRLQIQHVYR DPGSILSLLV
     LEIV