ID   KTNA_ASPNC              Reviewed;         303 AA.
AC   A2QK64;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Methyltransferase ktnA {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
DE   AltName: Full=Kotanin biosynthesis cluster protein A {ECO:0000303|PubMed:22945023};
GN   Name=ktnA {ECO:0000303|PubMed:22945023}; ORFNames=An04g09510;
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.
RX   PubMed=17315249; DOI=10.1002/cbic.200600434;
RA   Huettel W., Mueller M.;
RT   "Regio- and stereoselective intermolecular oxidative phenol coupling in
RT   kotanin biosynthesis by Aspergillus niger.";
RL   ChemBioChem 8:521-529(2007).
RN   [3]
RP   FUNCTION.
RX   PubMed=22945023; DOI=10.1002/anie.201203603;
RA   Gil Girol C., Fisch K.M., Heinekamp T., Guenther S., Huettel W., Piel J.,
RA   Brakhage A.A., Mueller M.;
RT   "Regio- and stereoselective oxidative phenol coupling in Aspergillus
RT   niger.";
RL   Angew. Chem. Int. Ed. 51:9788-9791(2012).
RN   [4]
RP   FUNCTION.
RX   PubMed=26389790; DOI=10.1021/jacs.5b06776;
RA   Mazzaferro L.S., Huettel W., Fries A., Mueller M.;
RT   "Cytochrome P450-catalyzed regio- and stereoselective phenol coupling of
RT   fungal natural products.";
RL   J. Am. Chem. Soc. 137:12289-12295(2015).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of the bicoumarin kotanin
CC       (PubMed:22945023, PubMed:26389790). The non-reducing polyketide
CC       synthase ktnS first catalyzes the formation of the pentaketidic 4,7-
CC       dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl
CC       coenzyme A molecules (PubMed:17315249, PubMed:22945023). Further O-
CC       methylation by ktnB leads to the formation of 7-demethylsiderin
CC       (PubMed:17315249, PubMed:22945023, PubMed:26389790). Then, an oxidative
CC       phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC
CC       forms the 8,8'-dimer P-orlandin via dimerization the monomeric
CC       precursor, 7-demethylsiderin (PubMed:26389790). P-orlandin is
CC       subsequently O-methylated in a stepwise fashion to demethylkotanin and
CC       kotanin (PubMed:22945023). The function of ktnA within the pathway has
CC       not been determined yet (PubMed:22945023).
CC       {ECO:0000269|PubMed:17315249, ECO:0000269|PubMed:22945023,
CC       ECO:0000269|PubMed:26389790}.
CC   -!- COFACTOR:
CC       Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000305}.
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DR   EMBL; AM270096; CAK47958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QK64; -.
DR   SMR; A2QK64; -.
DR   PaxDb; A2QK64; -.
DR   EnsemblFungi; CAK47958; CAK47958; An04g09510.
DR   VEuPathDB; FungiDB:An04g09510; -.
DR   HOGENOM; CLU_065416_0_0_1; -.
DR   Proteomes; UP000006706; Chromosome 6L.
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; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..303
FT                   /note="Methyltransferase ktnA"
FT                   /id="PRO_0000442166"
SQ   SEQUENCE   303 AA;  33246 MW;  4925CA02B4414128 CRC64;
     MTRTPAAPEK HNRDSASRYK SGSKISTLFA EELVERSAIA GFGRKDLVVF DNACGTGAIS
     SALHRALGDE KTRTWKLTCG DVSEAMVEVS KQKMIEEGWQ NAEVEVVDAQ NTGLLSDHYT
     HVFSAFGKML GTQGNGIMLT SISAFNLFPD DKAAMEECFR VLQSGGTLAV STWCSTVWAT
     LIQSAIASIP GDLPTPTTED IFGLYNKNWA DESRVRAQFQ QAGFTDINVT SVKKEYTVPV
     QELAEACKIS LPHITRKFWT QEQRDSYEAE VPKAVLRILE EEQRGIGLGA MKAEAIIATA
     RKP