ID   AUND_ASPNA              Reviewed;         424 AA.
AC   G3XSI5;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=O-methyltransferase aunD {ECO:0000303|PubMed:31067027};
DE            EC=2.1.1.- {ECO:0000305|PubMed:31067027};
DE   AltName: Full=Aurasperone B biosynthesis cluster protein D {ECO:0000303|PubMed:31067027};
GN   Name=aunD {ECO:0000303|PubMed:31067027}; ORFNames=ASPNIDRAFT_205346;
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, 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: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of aurasperone B, a dimeric gamma-naphthopyrone
CC       (PubMed:31067027). The first step in the biosynthesis of aurasperone B
CC       is the production of gamma-naphthopyrone precursor YWA1 by the non-
CC       reducing polyketide synthase albA, via condensation of one acetyl-CoA
CC       starter unit with 6 malonyl-CoA units (PubMed:31067027). YWA1 is then
CC       methylated by aunE at position C-6 to yield foncesin which is further
CC       methylated at position C-8 by aunD to produce fonsecin B (Probable). A
CC       key enzyme in the biosynthetic pathway is the cytochrome P450
CC       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   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:31067027}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the accumulatio of aurasperone B and
CC       fonsecin B. {ECO:0000269|PubMed:31067027}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; ACJE01000004; EHA27206.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XSI5; -.
DR   SMR; G3XSI5; -.
DR   EnsemblFungi; EHA27206; EHA27206; ASPNIDRAFT_205346.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1102571; -.
DR   HOGENOM; CLU_005533_1_4_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..424
FT                   /note="O-methyltransferase aunD"
FT                   /id="PRO_0000449889"
FT   ACT_SITE        326
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         275
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   424 AA;  46776 MW;  B7E875CFD9D59175 CRC64;
     MDDRLSSQLE RYASQVTASA TLIIRHLKSL KDEPSTLPSQ TSVPTAVGTA QLRLAEAAFQ
     LLHFTRDPGN VLTQLTVDLQ VISAVRWLLH FEIFSLVPLE GSISYHELSS VANVPENLLR
     SHIRLAMTCH LFQESGPIGM VAHSPVSCQL ASDPSLVSWG QYFANSVFPT ATKNVNATAA
     WPGSKALNET AHNLAFNHHG SFFDYVSQDP ARTVEFANSM KAVSTTSLFD TCHLCKSFDW
     SSLGDGVVVD MGGSTGHVSI ALAESFPSLR FVVQDLPDVV SNSIRQLEER QLPLSVTTRI
     QFQGHSLLHM QPVKGAAVYL LRQILHDWPD REAVQILRSI VPALGPRSKI FIADIVLPEA
     GSIPATEEQV MRCNDLLLHQ FTNTLERTLE DWQAIVSRVS DNLRIQHVYR DPGSILSLLV
     IETV