KTNB_ASPNC
ID KTNB_ASPNC Reviewed; 413 AA.
AC A2QK65;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=O-methyltransferase kntB {ECO:0000303|PubMed:22945023};
DE EC=2.1.1.- {ECO:0000305|PubMed:22945023};
DE AltName: Full=Kotanin biosynthesis cluster protein B {ECO:0000303|PubMed:22945023};
GN Name=ktnB {ECO:0000303|PubMed:22945023}; ORFNames=An04g09520;
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, DISRUPTION PHENOTYPE, AND PATHWAY.
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). {ECO:0000269|PubMed:17315249,
CC ECO:0000269|PubMed:22945023, ECO:0000269|PubMed:26389790}.
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22945023}.
CC -!- DISRUPTION PHENOTYPE: Leads to complete loss in coumarin biosynthesis
CC (PubMed:22945023). {ECO:0000269|PubMed:22945023}.
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; AM270096; CAK47959.1; -; Genomic_DNA.
DR RefSeq; XP_001402308.1; XM_001402271.1.
DR AlphaFoldDB; A2QK65; -.
DR SMR; A2QK65; -.
DR PaxDb; A2QK65; -.
DR EnsemblFungi; CAK47959; CAK47959; An04g09520.
DR GeneID; 4991355; -.
DR KEGG; ang:ANI_1_1410184; -.
DR VEuPathDB; FungiDB:An04g09520; -.
DR HOGENOM; CLU_005533_5_2_1; -.
DR Proteomes; UP000006706; Chromosome 6L.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:1900596; P:(+)-kotanin biosynthetic process; IMP:GO_Central.
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..413
FT /note="O-methyltransferase kntB"
FT /id="PRO_0000442168"
FT ACT_SITE 322
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 255..256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 302..303
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 319
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 413 AA; 46523 MW; 729BF1C853419B30 CRC64;
MTYPEEIDEY SLIQNGLKSL NEAAQRCQQT KHSSQDSSIE GCSARQSARD ELVLEALKFL
QIAQGPIDAA ATCYERTAHL ASVRALLEMG VFEALPTGRV SRRTEELARE LNVDESLLAR
LLRNSSLYGP FEETGPGQYR HTPFSEAYLR PEIRGMFRFA MDDHMPAHLK LHEFLQRNGW
QEPSSTTDNP YTYAHKTNGK SMFDNLSEKP ERMKAFNNGM TVQAMTPLWM IDLFPWRSLA
QLKPTAGQVL AVDIGGGKGK AISRIRSFCN GLPGRYILQD QEHVVKSVEG SLDPSIERMA
YNFFTEQPIR GAVTYLIRRC LHNWPQDSVV CILQNIAAAM EPGKSRLLIE EIVVPAEKAG
VEEGWMDMIM MSLGAKQRTL KEWEMVLGLA GLEVKKVYQI PGNCHGLIEA WLK
