AUNA_ASPNC
ID AUNA_ASPNC Reviewed; 305 AA.
AC A2QBE7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Aurasperone B biosynthesis cluster protein A {ECO:0000303|PubMed:31067027};
DE Flags: Precursor;
GN Name=aunA {ECO:0000303|PubMed:31067027}; ORFNames=An01g14980;
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, 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: Part of the gene cluster that mediates the biosynthesis of
CC aurasperone B, a dimeric gamma-naphthopyrone (PubMed:31067027). The
CC first step in the biosynthesis of aurasperone 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 aunE at
CC position C-6 to yield foncesin which is further methylated at position
CC C-8 by aunD to produce fonsecin B (Probable). A key enzyme in the
CC biosynthetic pathway is the cytochrome P450 monooxygenase aunB which
CC catalyzes the oxidative dimerization of fonsecin B to aurasperone B
CC (PubMed:31067027). AunB also catalyzes the oxidative dimerization of
CC rubrofusarin B into aurasperone A (PubMed:31067027).
CC {ECO:0000269|PubMed:31067027, ECO:0000305|PubMed:31067027}.
CC -!- SIMILARITY: Belongs to the bfoA family. {ECO:0000305}.
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DR EMBL; AM269994; CAK37452.1; -; Genomic_DNA.
DR RefSeq; XP_001389886.1; XM_001389849.1.
DR AlphaFoldDB; A2QBE7; -.
DR PaxDb; A2QBE7; -.
DR EnsemblFungi; CAK37452; CAK37452; An01g14980.
DR GeneID; 4978036; -.
DR KEGG; ang:ANI_1_3416014; -.
DR VEuPathDB; FungiDB:An01g14980; -.
DR HOGENOM; CLU_072152_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
PE 3: Inferred from homology;
KW Glycoprotein; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..305
FT /note="Aurasperone B biosynthesis cluster protein A"
FT /id="PRO_5002644895"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 305 AA; 34027 MW; 9EF7362CCB622A34 CRC64;
MSIFFSIRFW PAAISAAILW LPQVLGRSNG TAPNYTVEEL WKLETTFWDN FLYPANVEQM
EAINSTLFTQ DVQGRVDITR VFNGSELNTE YIFGLFSDPD HVSLVGVPVD YSITQFIAQG
NIASATTVVT FNATSFGNLL VPVTIDTWIM WDADGRIMQY DATFRWFGFL LDTLVEALAE
SINGTTSQAT ASLTQLLATT ICATHDQYCT GSNQQYDNNT ACLDFLTSAI PLGKDYELGR
NTLLCREVHE HMVQYDPALH CPHIGPTGGD YCVDDQTYAQ KVLQKYFNQS WIVGVPSTGD
IWLGD
