ID   ADAD_ASPNG              Reviewed;         249 AA.
AC   G3KLH3;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=O-methyltransferase adaD {ECO:0000303|PubMed:21866960};
DE            EC=2.1.1.- {ECO:0000269|PubMed:21866960};
DE   AltName: Full=2-acetyl-2-decarboxamidoanthrotainin biosynthesis cluster protein D {ECO:0000303|PubMed:21866960};
GN   Name=adaD {ECO:0000303|PubMed:21866960}; ORFNames=ATCC64974_92730;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, CATALYTIC
RP   ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 1015 / NV DSM 2061;
RX   PubMed=21866960; DOI=10.1021/ja206906d;
RA   Li Y., Chooi Y.H., Sheng Y., Valentine J.S., Tang Y.;
RT   "Comparative characterization of fungal anthracenone and naphthacenedione
RT   biosynthetic pathways reveals an alpha-hydroxylation-dependent Claisen-like
RT   cyclization catalyzed by a dimanganese thioesterase.";
RL   J. Am. Chem. Soc. 133:15773-15785(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64974 / FGSC A733 / N402;
RX   PubMed=30319579; DOI=10.3389/fmicb.2018.02269;
RA   Laothanachareon T., Tamayo-Ramos J.A., Nijsse B., Schaap P.J.;
RT   "Forward genetics by genome sequencing uncovers the central role of the
RT   Aspergillus niger goxB locus in hydrogen peroxide induced glucose oxidase
RT   expression.";
RL   Front. Microbiol. 9:2269-2269(2018).
CC   -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y
CC       receptor antagonist (PubMed:21866960). The decaketide backbone of TAN-
CC       1612 is synthesized by the non-reducing polyketide synthase adaA via
CC       condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units.
CC       The FAD-dependent monooxygenase adaC then performs hydroxylation at C2
CC       while the polaketide chain is still attached to the NRPKS adaA
CC       (PubMed:21866960). The alpha-hydroxylation step at C2 appears to be
CC       crucial for the following C18-C1 Claisen cyclization and release of the
CC       C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps
CC       performed by the lactamase-like protein adaB (PubMed:21866960).
CC       Finally, the O-methyltransferase adaD performs the C9 O-methylation to
CC       complete the biosynthesis of TAN-1612 (PubMed:21866960).
CC       {ECO:0000269|PubMed:21866960}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-acetyl-3,4a,8,10,11,12a-hexahydroxy-1,4,4a,5,12,12a-
CC         hexahydrotetracene-1,12-dione + S-adenosyl-L-methionine = H(+) + S-
CC         adenosyl-L-homocysteine + TAN-1612; Xref=Rhea:RHEA:64100,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:146217, ChEBI:CHEBI:146218;
CC         Evidence={ECO:0000269|PubMed:21866960};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64101;
CC         Evidence={ECO:0000269|PubMed:21866960};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:21866960}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JN257714; AEN83886.1; -; Genomic_DNA.
DR   EMBL; OGUI01000016; SPB51663.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3KLH3; -.
DR   STRING; 5061.CADANGAP00008890; -.
DR   VEuPathDB; FungiDB:An11g07340; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1139200; -.
DR   VEuPathDB; FungiDB:ATCC64974_92730; -.
DR   VEuPathDB; FungiDB:M747DRAFT_298770; -.
DR   OrthoDB; 1170760at2759; -.
DR   Proteomes; UP000236662; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Transferase.
FT   CHAIN           1..249
FT                   /note="O-methyltransferase adaD"
FT                   /id="PRO_0000446349"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  28306 MW;  D1EE5606ED7740EE CRC64;
     MSSVTLTTTT TTTSTPPKPT PKDEPQEQIY TPWRLFIYDI WVLGIVSTLA WGCRISTYLI
     PLFRSNVGKK HLDIGAGTGY YLNQARISST TQLTIVDNET HALNVALARC KHPVTQTHGI
     VTDILQPSPF PETYLTNNDQ KFDSVSMYYL LHCLPVPVAS KCKIFTHLKK YMTEDGVVHG
     ANVLGKGVRK DNWFARIIRR GCLNHGVFHN EEDNAYEFER ALRENFWEVE TWVVGSVFVF
     RAKRPILDA