ID   AUNA_ASPNA              Reviewed;         305 AA.
AC   G3XSI2;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Aurasperone B biosynthesis cluster protein A {ECO:0000303|PubMed:31067027};
DE   Flags: Precursor;
GN   Name=aunA {ECO:0000303|PubMed:31067027};
GN   ORFNames=ASPNIDRAFT_35374 {ECO:0000312|EMBL:EHA27203.1};
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, 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; ACJE01000004; EHA27203.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XSI2; -.
DR   EnsemblFungi; EHA27203; EHA27203; ASPNIDRAFT_35374.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1162950; -.
DR   HOGENOM; CLU_072152_0_0_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
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_5003460058"
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;  34011 MW;  A9694FD2AB711827 CRC64;
     MSIFFSIRFW PAAISAAILW LPQVLGRSNG TAPNYTVEEL WKLETTFWDN FLYPANVEQM
     EAINSTLFTQ DVQGRVDITR VFNGSELNTE YIFGLFSDPD HVSLVGVPVD YSITQFIAQG
     NIASATTVVT FNATSFGNLL VPVTIDTWIM WDADGRIMQY DATFRWFGFL LDTLVEALAE
     SINGTTSQAT ASLTQLLATT ICATHDQYCT GANQQYDNNT ACLDFLTSAI PLGKDYELGR
     NTLLCREVHE HMVQYDPALH CPHIGPTGGD YCVDDQTYAQ KVLQKYFNQS WIVGVPSTGD
     IWLGD