AUNB_ASPNA
ID AUNB_ASPNA Reviewed; 159 AA.
AC G3XSI3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
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};
DE Flags: Fragment;
GN Name=aunB {ECO:0000303|PubMed:31067027};
GN ORFNames=ASPNIDRAFT_136667 {ECO:0000312|EMBL:EHA27204.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC 328 / USDA 3528.7;
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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}.
CC -!- CAUTION: The sequence misses both the N-terminal and C-terminal parts.
CC The correct gene model with the complete protein sequence could not be
CC recovered from the submitted genomic sequence. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACJE01000004; EHA27204.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XSI3; -.
DR SMR; G3XSI3; -.
DR EnsemblFungi; EHA27204; EHA27204; ASPNIDRAFT_136667.
DR HOGENOM; CLU_001570_14_7_1; -.
DR Proteomes; UP000009038; 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 Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN <1..>159
FT /note="Cytochrome P450 monooxygenase aunB"
FT /id="PRO_0000449885"
FT BINDING 134
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 NON_TER 1
FT /evidence="ECO:0000312|EMBL:EHA27204.1"
FT NON_TER 159
FT /evidence="ECO:0000312|EMBL:EHA27204.1"
SQ SEQUENCE 159 AA; 18003 MW; 00DFC2F01068012B CRC64;
TADNMLNALF YFLLRNPQCL KRLEEEVSCV GATVNELSDD RLAKLPYLNA CINETFRIAP
AFNGGILQRV SCGATVDGVY VPPGVAVSVD HYTLGHDPQY WVKPDVFNPE RWIDPDCKDN
FKASRPFLIG ARQCPGRQMA YQMFRVCVAK LVYLYTFEL
