DPFGK_GIBZE
ID DPFGK_GIBZE Reviewed; 298 AA.
AC I1RL12; A0A098DL06;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=S-adenosyl-L-methionine-dependent methyltransferase dpfgK {ECO:0000303|PubMed:32286350};
DE EC=2.1.1.- {ECO:0000269|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein K {ECO:0000303|PubMed:32286350};
GN Name=dpfgK {ECO:0000303|PubMed:32286350};
GN ORFNames=FG04589, FGRAMPH1_01T15649;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOTECHNOLOGY.
RX PubMed=32286350; DOI=10.1038/s41467-020-15664-4;
RA Tsukada K., Shinki S., Kaneko A., Murakami K., Irie K., Murai M.,
RA Miyoshi H., Dan S., Kawaji K., Hayashi H., Kodama E.N., Hori A., Salim E.,
RA Kuraishi T., Hirata N., Kanda Y., Asai T.;
RT "Synthetic biology based construction of biological activity-related
RT library of fungal decalin-containing diterpenoid pyrones.";
RL Nat. Commun. 11:1830-1830(2020).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase; part of
CC the gene cluster that mediates the biosynthesis of diterpenoid pyrones
CC (PubMed:32286350). The first step of the pathway is the synthesis of
CC the alpha-pyrone moiety by the polyketide synthase dpfgA via
CC condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units
CC and 2 methylations (Probable). The alpha-pyrone is then combined with
CC geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpfgD
CC through the action of the prenyltransferase dpfgC to yield a linear
CC alpha-pyrone diterpenoid (Probable). Subsequent steps in the
CC diterpenoid pyrone biosynthetic pathway involve the decalin core
CC formation, which is initiated by the epoxidation of the C10-C11 olefin
CC by the FAD-dependent oxidoreductase dpfgE, and is followed by a
CC cyclization cascade catalyzed by the terpene cyclase dpfgB (Probable).
CC The short chain dehydrogenase/reductase dpfgG then oxidizes the 8S
CC hydroxy group to a ketone and the short chain dehydrogenase/reductase
CC dpfgH reduces the ketone to the 8R hydroxy group to yield higginsianin
CC B (PubMed:32286350). Higginsianin B is further methylated by the
CC methyltransferase dpfgI to produce the intermediate named FDDP B
CC (PubMed:32286350). The cytochrome P450 monooxygenase dfgpJ then
CC catalyzes a three-step oxidation at C-27 to generate a carboxylic acid
CC as well as C-26 hydroxylation (PubMed:32286350). Finally,
CC methyltransferase dpfgK methylates the carboxylic acid generated by
CC dpfgJ, yielding the final diterpenoid pyrones from the pathway which
CC were named FDDP D and FDDP E (PubMed:32286350).
CC {ECO:0000269|PubMed:32286350, ECO:0000305|PubMed:32286350}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:32286350}.
CC -!- BIOTECHNOLOGY: Diterpenoid pyrones display various biological
CC activities and FDDP E shows anti-HIV activity (PubMed:32286350). FDDP D
CC and FDDP E show also inhibitory activity of 42-mer-amyloid beta
CC aggregation that is involved in the pathogenesis of Alzheimer's disease
CC (PubMed:32286350). {ECO:0000269|PubMed:32286350}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; HG970333; CEF79624.1; -; Genomic_DNA.
DR RefSeq; XP_011320992.1; XM_011322690.1.
DR AlphaFoldDB; I1RL12; -.
DR SMR; I1RL12; -.
DR STRING; 5518.FGSG_04589P0; -.
DR GeneID; 23551828; -.
DR KEGG; fgr:FGSG_04589; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G15649; -.
DR eggNOG; ENOG502RXVR; Eukaryota.
DR HOGENOM; CLU_069348_2_0_1; -.
DR InParanoid; I1RL12; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016874; TcmP-like.
DR Pfam; PF04072; LCM; 1.
DR PIRSF; PIRSF028177; Polyketide_synth_Omtfrase_TcmP; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..298
FT /note="S-adenosyl-L-methionine-dependent methyltransferase
FT dpfgK"
FT /id="PRO_0000451558"
SQ SEQUENCE 298 AA; 34253 MW; 2BEE69C037A21B4D CRC64;
MSGSTLDKGK VTLTGAEETL LITLFARAKD AESPNPVLND QYSAQVVSRI RDQGYNFSRT
TLDRSDSSFF TSLVATRARV LDICCEQFLE RNPGPATIIH LACGMDSRSL RLKWQGEGRL
WIDADRQDVI KLRRQIMDEP APERGEYRLT DPDIHDDAWL RDYNVPTDRP VLVLFEGLTP
YLTRDEVVSL LRRITNHFRD SGVNGEIRFD APGSISYFLI NYVFNKPLRS MGTQFTWYMD
DPRELETHVP GLKYRERMFV LHDYARLGNY GWLAGFLLRV ADWFNIGGRI GSGYGYEF
