KTND_ASPNC
ID KTND_ASPNC Reviewed; 608 AA.
AC A2QK68;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=FAD-binding monooxygenase ktnD {ECO:0000305};
DE EC=1.14.13.- {ECO:0000305};
DE AltName: Full=Kotanin biosynthesis cluster protein D {ECO:0000303|PubMed:22945023};
GN Name=ktnD {ECO:0000303|PubMed:22945023}; ORFNames=An04g09550;
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 ktnD 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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:H3JQW0};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:H3JQW0};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AM270096; CAK47962.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QK68; -.
DR SMR; A2QK68; -.
DR PaxDb; A2QK68; -.
DR EnsemblFungi; CAK47962; CAK47962; An04g09550.
DR VEuPathDB; FungiDB:An04g09550; -.
DR HOGENOM; CLU_006937_7_1_1; -.
DR Proteomes; UP000006706; Chromosome 6L.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..608
FT /note="FAD-binding monooxygenase ktnD"
FT /id="PRO_0000442171"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 56..59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 66..68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 68..69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 74
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 201..207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 224..225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 608 AA; 68531 MW; 5D75B72A69909FFB CRC64;
MPSNYTQHVG NHDFTRATVV IIGAGVSGMC MAIDLLHRTP IRKFVILEQG SSVGGTWANN
LYPGCASDVC SSLYSYSFEQ RPDWAAEYPG QEEFLTYMTD VAQKHGLYKY IRFNSTVQEA
RWDDKQQQWK VKVALNSAKA SEFHEQYELT TNFLVSAVGQ LNVPSYPSIS GLDDYTGKLI
HSARWDWTYD FSGKRIGVIG NGASAIQIVP ELAKTASHIT IYQRSPKWLL PRSNKKIGAI
QHFLLSYVPP LRWCKRILQM RYREWLYNVL VTPGTVPARQ FEAQSQEWMK SQLPDKPELW
DTLTPNYAIG CKRVLISDDF YAALNASHVD LNTRPIQRIT ATGVQTDDDE QEYDLIVLAT
GFRASEFLHP IRVYGAGGRS LEDIWKDGPR AYYGMTVEDV PNFGMLYGPN TNLGHNSVIT
MIEAQSRYLS TMIRAVADAK KKDQTLVIQP RPEVLREYNE RVQKHLAETS FADPNCQSWY
KTDEGLITNN WPSTVVRYQK EVSQVRWADF ILKGSGSAAV AKKKATYVGR VKEEALVSNV
TLFLGVALAA GGVYWRATSW WKWEVPLIDK VGDDGILYGS GKTAWTSRVC PGAHCASGLL
RILSLRRA
