BFOB_ASPBC
ID BFOB_ASPBC Reviewed; 489 AA.
AC A0A1L9URA0;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Cytochrome P450 monooxygenase bfoB {ECO:0000303|PubMed:31067027};
DE EC=1.-.-.- {ECO:0000269|PubMed:31067027};
DE AltName: Full=Bifonsecin B biosynthesis cluster protein B {ECO:0000303|PubMed:31067027};
DE Flags: Precursor;
GN Name=bfoB {ECO:0000303|PubMed:31067027}; ORFNames=ASPBRDRAFT_192866;
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, CATALYTIC ACTIVITY, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 fonsecin B + H(+) + NADPH + O2 = bifonsecin B + 2 H2O +
CC NADP(+); Xref=Rhea:RHEA:62784, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:133825, ChEBI:CHEBI:145921;
CC Evidence={ECO:0000269|PubMed:31067027};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62785;
CC Evidence={ECO:0000269|PubMed:31067027};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H(+) + NADPH + O2 + 2 rubrofusarin B = 2 H2O + NADP(+) +
CC nigerone; Xref=Rhea:RHEA:62792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:145920, ChEBI:CHEBI:145950;
CC Evidence={ECO:0000269|PubMed:31067027};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62793;
CC Evidence={ECO:0000269|PubMed:31067027};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31067027}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KV878681; OJJ74130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9URA0; -.
DR SMR; A0A1L9URA0; -.
DR EnsemblFungi; OJJ74130; OJJ74130; ASPBRDRAFT_192866.
DR VEuPathDB; FungiDB:ASPBRDRAFT_192866; -.
DR OrthoDB; 467733at2759; -.
DR Proteomes; UP000184499; Unassembled WGS sequence.
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; 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.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..489
FT /note="Cytochrome P450 monooxygenase bfoB"
FT /id="PRO_0000448921"
FT BINDING 429
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"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 489 AA; 55302 MW; D7FCD9E7A29BBEF2 CRC64;
MLALYLIAGL LVGLLVYRLH LDPLSHIPGP FLAKFIPICN IRMLHTGRIV FTFRELHDTY
GPVVRIGPSE LSFATVTAFD SIYGFEGEKK FTIYGSRRGV VSSASGTDES LGNATSKESR
RKLRPLITST LNELMASSAE EYCHLALTEQ LAAHRVGQDG STPISLSTLN YRYLWQLANM
VAFGNRGQEA HRETFNPHIR WPSPFVSFID LLFIFCSRAT IQQHARTAYK AWQAIRFVCR
QTTQGPQVDF IADDSTFPDN LHRRLRQAAE KAGLDDVSDF TLLVNSMILR FSVYGTSDHM
INAVFYYLLR HPQCLKRLEK EVLNAGTSVE ELSDNRLAKL PYLNACINET FRISPAFNGG
ILQRVSCGAT VDGVYVPPGV AVTVDNYTLG RSKQYWENPD AFCPERWLES SDKNVFKASR
PFLIGSRQCP GRQMAYQMFR ILVAKLVYLY SMELVNKDFD IERDTFCGLH WADLEVDAIL
KPRTDVLGY
