PYNC_ASPNC
ID PYNC_ASPNC Reviewed; 363 AA.
AC A5ABG3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Methyltransferase pynC {ECO:0000303|PubMed:24106156};
DE EC=2.1.1.- {ECO:0000269|PubMed:26414728};
DE AltName: Full=Pyranonigrin biosynthesis cluster protein C {ECO:0000303|PubMed:24106156};
GN Name=pynC {ECO:0000303|PubMed:24106156}; ORFNames=An11g00280;
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, AND INDUCTION.
RX PubMed=24106156; DOI=10.1002/cbic.201300430;
RA Awakawa T., Yang X.L., Wakimoto T., Abe I.;
RT "Pyranonigrin E: a PKS-NRPS hybrid metabolite from Aspergillus niger
RT identified by genome mining.";
RL ChemBioChem 14:2095-2099(2013).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=26414728; DOI=10.1021/acs.orglett.5b02435;
RA Yamamoto T., Tsunematsu Y., Noguchi H., Hotta K., Watanabe K.;
RT "Elucidation of pyranonigrin biosynthetic pathway reveals a mode of
RT tetramic acid, fused gamma-pyrone, and exo-methylene formation.";
RL Org. Lett. 17:4992-4995(2015).
CC -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC biosynthesis of pyranonigrins, a family of antioxidative compounds
CC (PubMed:24106156, PubMed:26414728). The first step of pyranonigrins
CC biosynthesis is performed by the hybrid PKS-NRPS synthetase that
CC condenses 6 malonyl-CoA units to an acetyl starter unit, to form a
CC 1,3,5-trioxotetradecane-6,8-dienyl-ACP (PubMed:24106156). The enoyl
CC reducrase (ER) domain of pynA is likely to be functional during the
CC first two rounds of polyketide chain extension, to generate the
CC saturated C-C bonds of the alkyl side chain (Probable). PynA
CC subsequently forms the amide bond between the acyl chain and L-serine
CC (PubMed:24106156, PubMed:26414728). Although pynA has a terminal
CC reductase domain, it appears to require the thioesterase pynI for the
CC release of the straight-chain intermediate from pynA via the formation
CC of a tetramic acid pyranonigrin J (PubMed:26414728). The
CC methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I
CC via N-methylation (PubMed:26414728). The FAD-dependent monooxygenase
CC pynG catalyzes an epoxidation-mediated cyclization to form the dihydro-
CC gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the
CC alcohol to the ketone and enolization to yield the characteristic
CC tetramic acid-fused gamma-pyrone core of pyranonigrin H
CC (PubMed:26414728). Pyranonigrin H is substrate of pynH for dehydration-
CC mediated exo-methylene formation from the serine side chain to produce
CC pyranonigrin E, before the oxidase pynE reduces the exo-methylene of
CC pyranonigrin E into a pendant methyl to form pyranonigrin G
CC (PubMed:26414728). The FAD-linked oxidoreductase pynB performs the
CC reverse reaction and converts pyranonigrin G back to pyranonigrin E
CC (PubMed:26414728). {ECO:0000269|PubMed:24106156,
CC ECO:0000269|PubMed:26414728, ECO:0000305|PubMed:24106156}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26414728}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor pynR. {ECO:0000269|PubMed:24106156}.
CC -!- DISRUPTION PHENOTYPE: Leads to a small accumulation of pyranonigrin J
CC and the formation of a desmethylated product pyranonigrin K.
CC {ECO:0000269|PubMed:26414728}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AM270218; CAK48261.1; -; Genomic_DNA.
DR RefSeq; XP_001394032.1; XM_001393995.1.
DR AlphaFoldDB; A5ABG3; -.
DR SMR; A5ABG3; -.
DR PaxDb; A5ABG3; -.
DR EnsemblFungi; CAK48261; CAK48261; An11g00280.
DR GeneID; 4984229; -.
DR KEGG; ang:ANI_1_1534094; -.
DR VEuPathDB; FungiDB:An11g00280; -.
DR HOGENOM; CLU_005533_5_2_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019748; P:secondary metabolic process; IGC:AspGD.
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 PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..363
FT /note="Methyltransferase pynC"
FT /id="PRO_0000450057"
FT BINDING 199..200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 254..255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 271
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 363 AA; 40300 MW; 1EB30BF714E3153F CRC64;
MSPSTINPES SPLHTYYFSM VEMSIMKLFL DHKIFTLIPT TPGASIPVTT LTTTLNASPS
LLTRLTNFLI ASGVLSSPQP GHIAHTPKSL QFTDPTSYQA LFFAHIFDFF LVPAVKWPGY
MAEHGLNEPT SASRTPFGYA AGYPDKTLYE ILETMPKRAA QFNATMAASF QPMPVLGMYD
FSWIEKLADE ERMAIVDVGG GKGQALKEIL GAYPGIRPEQ CVLFDVDDVI REAVAEAERD
DDETWRTVRK IPGSFFSEQP VKGAAVYHIR RVLNDWPDED CVTILRRIRD AAAPNSRVLI
SEQILQEEPS LAVAALDLWM LNFGGKRRSE GMFGELAQRT GWKVNGVFRD KESDTGVVEL
VVA
