AUND_ASPNC
ID AUND_ASPNC Reviewed; 424 AA.
AC A2QBF0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 63.
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=An01g15010;
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, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK37455.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM269994; CAK37455.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001389889.2; XM_001389852.2.
DR AlphaFoldDB; A2QBF0; -.
DR SMR; A2QBF0; -.
DR PaxDb; A2QBF0; -.
DR EnsemblFungi; CAK37455; CAK37455; An01g15010.
DR GeneID; 4977054; -.
DR KEGG; ang:ANI_1_2036014; -.
DR VEuPathDB; FungiDB:An01g15010; -.
DR HOGENOM; CLU_005533_1_4_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
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; IPR036388; WH-like_DNA-bd_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_0000449890"
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; 46741 MW; CAFE3593A8E94E36 CRC64;
MDDRLSSQLE HYASQVTASA TLIIRHLKSL KDEPSTLPSQ TSVPTAVGTA QLRLAEAAFQ
LLHFTRDPGN VLTQLTVDLQ VISAVRWLLH FEIFSLVPLE GSISYHELSS VANVPENLLR
SHIRLAMTCH LFQESGPIGM VAHSPVSRQL ASDPSLVSWG QYFANSVFPT ATKNVNATAA
WPGSKALNET AHNLAFNHHG SFFDYVSQDP ARTVEFANSM KAVSTTSLFD TCHLCKSFDW
SSLGDGVVVD MGGSTGHVSI ALAESFPSLR FVVQDLPDVV SNSIRQLEER QLPLSVTTRI
QFQGHSLLHM QPVKGAAVYL LRQILHDWPD REAVQILRSI VPALGPSSKI FIADIVLPEA
GSIPATEEQV MRCNDLLLHQ FTNTLERTLE DWQAIVSRVS DNLRIQHVYR DPGSILSLLV
IETV
