AUNE_ASPNC
ID AUNE_ASPNC Reviewed; 386 AA.
AC A2QBF1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=O-methyltransferase aunE {ECO:0000303|PubMed:31067027};
DE EC=2.1.1.- {ECO:0000305|PubMed:31067027};
DE AltName: Full=Aurasperone B biosynthesis cluster protein E {ECO:0000303|PubMed:31067027};
GN Name=aunE {ECO:0000303|PubMed:31067027}; ORFNames=An01g15020;
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: 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 -!- 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; AM269994; CAK37456.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QBF1; -.
DR SMR; A2QBF1; -.
DR PaxDb; A2QBF1; -.
DR EnsemblFungi; CAK37456; CAK37456; An01g15020.
DR VEuPathDB; FungiDB:An01g15020; -.
DR HOGENOM; CLU_064550_0_0_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; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00891; Methyltransf_2; 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..386
FT /note="O-methyltransferase aunE"
FT /id="PRO_0000449892"
FT ACT_SITE 299
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 386 AA; 43053 MW; 0CCB4AB38C2B3BD4 CRC64;
MAAPQNAPIP EAGKKVMSTV TLAPALGFVP IAVHFDLFGC LQEIGKPATA QDVCNFHHTK
YGDTDLFSIT FLHNKSMFAK VNRTSDDTLF LMGGLGFLDL LPDDVYQANA VTRFLVDTPS
AQHGAMHFTS EGLLASAFLM RRLMDTKFEY PFQECDTPFQ YAHKLMGNDH LAREHVYSVM
HETGRLDSFN TFMTGKFGRW GTMPDRVRKL GYDLDGLLQS TAPERIRVVD IGGGRGELLL
EMQATYPHLL KKENLILQEY NADIGVVPEV TEMGWNYKED ASEQPVKGAL LYSMAHVLHN
LSDIESIKLL NKVSRVMAPS SRLLIQEFTK NAASSTTHAA MILMHAGRER TSAEWRDLAA
FAGLEITFEA YPPNGECVVE MRKVLN
