BFOA_ASPBC
ID BFOA_ASPBC Reviewed; 297 AA.
AC A0A1L9UR45;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Bifonsecin B biosynthesis cluster protein A {ECO:0000303|PubMed:31067027};
DE Flags: Precursor;
GN Name=bfoA {ECO:0000303|PubMed:31067027}; ORFNames=ASPBRDRAFT_145890;
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.
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: Part of the gene cluster that mediates the biosynthesis of
CC bifonsecin B, a dimeric gamma-naphthopyrone (PubMed:31067027). The
CC first step in the biosynthesis of bifonsecin B is the production of
CC gamma-naphthopyrone precursor YWA1 by the non-reducing polyketide
CC synthase albA, via condensation of one acetyl-CoA starter unit with 6
CC malonyl-CoA units (PubMed:31067027). YWA1 is then methylated by bfoE at
CC position C-6 to yield foncesin which is further methylated at position
CC C-8 by bfoD to produce fonsecin B (Probable). A key enzyme in the
CC biosynthetic pathway is the cytochrome P450 monooxygenase bfoB which
CC catalyzes the oxidative dimerization of fonsecin B to bifonsecin B
CC (PubMed:31067027). Bfob also catalyzes the oxidative dimerization of
CC rubrofusarin B into nigerone (PubMed:31067027). The stereoselectivity
CC of bfoB is influenced by the two natural monomeric substrates;
CC homodimerization of fonsecin B yields a stereochemically pure biaryl,
CC M-foncerine B, while rubrofusarin B yields a mixture of enantiomers
CC M- and P-nigerone (PubMed:31067027). The function of bfoA within the
CC bifonsecin B biosynthesis pathway has not been determined yet
CC (Probable). {ECO:0000269|PubMed:31067027, ECO:0000305|PubMed:31067027}.
CC -!- SIMILARITY: Belongs to the bfoA family. {ECO:0000305}.
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DR EMBL; KV878681; OJJ74131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9UR45; -.
DR EnsemblFungi; OJJ74131; OJJ74131; ASPBRDRAFT_145890.
DR VEuPathDB; FungiDB:ASPBRDRAFT_145890; -.
DR OrthoDB; 1186411at2759; -.
DR Proteomes; UP000184499; Unassembled WGS sequence.
PE 3: Inferred from homology;
KW Glycoprotein; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..297
FT /note="Bifonsecin B biosynthesis cluster protein A"
FT /evidence="ECO:0000255"
FT /id="PRO_5012724922"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 297 AA; 33107 MW; 922B5E79ED59F260 CRC64;
MHFWWTAISA GLLCLPQALG RSDSPNYTVE ELWKLETTFW DNFLYPANVE QMEAINSTLF
TPDVQGRVDI TRVFNGSELN TEYIFGLFSD PDHVSLVGVP VDYSIVQFIA QGNIASATTV
VTFNATSFGN LLIPVTIDTW IMWDSNGQIV QYDATFRWFG FLLDTLVETL AASINGTTSE
ATAALTQLLA TTICATHDQY CTGANQQYDN NTACYDFLTT AIPLGKDYEL GRNTLLCREV
HEHMVQYDPA LHCPHIGPTG GDYCVDDQTY AQKVLQKYFN QSWIVGVPST GDIWLGD
