AUNB_ASPNC
ID AUNB_ASPNC Reviewed; 447 AA.
AC A2QBE8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cytochrome P450 monooxygenase aunB {ECO:0000303|PubMed:31067027};
DE EC=1.-.-.- {ECO:0000269|PubMed:31067027};
DE AltName: Full=Aurasperone B biosynthesis cluster protein B {ECO:0000303|PubMed:31067027};
GN Name=aunB {ECO:0000303|PubMed:31067027}; ORFNames=An01g14990;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, 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 aurasperone B, a dimeric gamma-
CC naphthopyrone (PubMed:31067027). The first step in the biosynthesis of
CC aurasperone B is the production of gamma-naphthopyrone precursor YWA1
CC by 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 aunE at position C-6 to yield foncesin which
CC is further methylated at position C-8 by aunD to produce fonsecin B
CC (Probable). A key enzyme in the biosynthetic pathway is the cytochrome
CC P450 monooxygenase aunB which catalyzes the oxidative dimerization of
CC fonsecin B to aurasperone B (PubMed:31067027). AunB also catalyzes the
CC oxidative dimerization of rubrofusarin B into aurasperone A
CC (PubMed:31067027). {ECO:0000269|PubMed:31067027,
CC ECO:0000305|PubMed:31067027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 fonsecin B + H(+) + NADPH + O2 = aurasperone B + 2 H2O +
CC NADP(+); Xref=Rhea:RHEA:62788, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:133756, ChEBI:CHEBI:133825;
CC Evidence={ECO:0000269|PubMed:31067027};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62789;
CC Evidence={ECO:0000269|PubMed:31067027};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + 2 rubrofusarin B = aurasperone A + 2 H2O +
CC NADP(+); Xref=Rhea:RHEA:62796, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:145920, ChEBI:CHEBI:146001;
CC Evidence={ECO:0000269|PubMed:31067027};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62797;
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 -!- DISRUPTION PHENOTYPE: Leads to the accumulation of the monomeric
CC compounds fonsecin B and flavasperone. {ECO:0000269|PubMed:31067027}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AM269994; CAK37453.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QBE8; -.
DR SMR; A2QBE8; -.
DR PaxDb; A2QBE8; -.
DR EnsemblFungi; CAK37453; CAK37453; An01g14990.
DR VEuPathDB; FungiDB:An01g14990; -.
DR HOGENOM; CLU_001570_14_11_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
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 Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..447
FT /note="Cytochrome P450 monooxygenase aunB"
FT /id="PRO_0000449886"
FT BINDING 386
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 447 AA; 50538 MW; 0CDD773A3181A3F2 CRC64;
MVGWLIYRLH LDPLSRIPGP LLAKFVPICN IRMVLTGRMM FTFKELHDTY GPVVRIGPSE
LSFATHSAFD TIYGPYGDKN FSLYGSRKGL LGSLDKENRR KLRPLVATSL NELLAAKGEE
YCHLAMDEQL ASHHVGQTEA TPVSLSTLNN RYLWQFASMA ANGNCGDETD RGTSFTNIFM
GLSFMALTQV IAICFIFRQP VHPGEVNYDR DESPFPDNLH SRLQQAASRT SLHVPEYLLQ
INCFVLRFSI YGTADNMLNA LFYFLLRNPQ CLKRLEEEVS CVGATVNELS DDRLAKLPYL
NACINETFRI APAFNGGILQ RVSCGATVDG VYVPPGVAVS VDHYTLGHDP QYWVKPDVFN
PERWIDPDCK DNFKASRPFL IGARQCPGRQ MAYQMFRVCV AKLVYLYTFE LLNKDFDIER
DTFSSYHWTG VKLDVTMKPR TPGVLGY
