ID   AUNE_ASPNA              Reviewed;         347 AA.
AC   G3XSI6;
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 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};
DE   Flags: Fragment;
GN   Name=aunE {ECO:0000303|PubMed:31067027}; ORFNames=ASPNIDRAFT_124971;
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: 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}.
CC   -!- CAUTION: The sequence misses the N-terminal part. The correct gene
CC       model with the complete protein sequence could not be recovered from
CC       the submitted genomic sequence. {ECO:0000305}.
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DR   EMBL; ACJE01000004; EHA27207.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XSI6; -.
DR   SMR; G3XSI6; -.
DR   EnsemblFungi; EHA27207; EHA27207; ASPNIDRAFT_124971.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_124971; -.
DR   HOGENOM; CLU_064550_0_0_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   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..347
FT                   /note="O-methyltransferase aunE"
FT                   /id="PRO_0000449891"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:EHA27207.1"
SQ   SEQUENCE   347 AA;  38727 MW;  D8A4F1E7A0ECFAD6 CRC64;
     APALGFVPIA VHFDLFGCLQ EIGKPATAQD VCISITFLHK KSMFAKVNRS SDDTLFLMGG
     LGFLDLLPDD VYQANAVTRF LVDTPSAQHG AMHFTSEGLL ASAFLMRRLM DTKFEYPFQE
     CDTPFQYAHK LMGNEHLARE HVYSVMHETG RLDSFNTFMT GKFGRWGTMP DRVRKLGYDL
     DGLLQSTAPE RIRVVDIGGG RGELLLEMQA TYPHLLKKEN LILQEYNADI GVVPEVTEMG
     WNYKEDASEQ PVKGALLYSM AHVLHNLSDI ESIKLLTKVA RVMAPSSRLL IQEFTKNAAS
     STTHAAMILM HAGRERTSAE WRDLAAFAGL EITFEAYPPN GECVVEM