DPFGI_GIBZE
ID DPFGI_GIBZE Reviewed; 378 AA.
AC I1RL18; A0A098DNU6;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=O-methyltransferase dpfgI {ECO:0000303|PubMed:32286350};
DE EC=2.1.1.- {ECO:0000269|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein I {ECO:0000303|PubMed:32286350};
GN Name=dpfgI {ECO:0000303|PubMed:32286350};
GN ORFNames=FG04596, FGRAMPH1_01T15663;
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: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of diterpenoid pyrones (PubMed:32286350). The first
CC step of the pathway is the synthesis of the alpha-pyrone moiety by the
CC polyketide synthase dpfgA via condensation of one acetyl-CoA starter
CC unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-
CC pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed
CC by the GGPP synthase dpfgD through the action of the prenyltransferase
CC dpfgC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent
CC steps in the diterpenoid pyrone biosynthetic pathway involve the
CC decalin core formation, which is initiated by the epoxidation of the
CC C10-C11 olefin by the FAD-dependent oxidoreductase dpfgE, and is
CC followed by a cyclization cascade catalyzed by the terpene cyclase
CC dpfgB (Probable). The short chain dehydrogenase/reductase dpfgG then
CC oxidizes the 8S hydroxy group to a ketone and the short chain
CC dehydrogenase/reductase dpfgH reduces the ketone to the 8R hydroxy
CC group to yield higginsianin B (PubMed:32286350). Higginsianin B is
CC further methylated by the methyltransferase dpfgI to produce the
CC intermediate named FDDP B (PubMed:32286350). The cytochrome P450
CC monooxygenase dfgpJ then catalyzes a three-step oxidation at C-27 to
CC generate a carboxylic acid as well as C-26 hydroxylation
CC (PubMed:32286350). Finally, methyltransferase dpfgK methylates the
CC carboxylic acid generated by dpfgJ, yielding the final diterpenoid
CC pyrones from the pathway which were named FDDP D and FDDP E
CC (PubMed:32286350). {ECO:0000269|PubMed:32286350,
CC 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 class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; HG970333; CEF79631.1; -; Genomic_DNA.
DR RefSeq; XP_011320984.1; XM_011322682.1.
DR AlphaFoldDB; I1RL18; -.
DR SMR; I1RL18; -.
DR GeneID; 23551834; -.
DR KEGG; fgr:FGSG_04596; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G15663; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_5_0_1; -.
DR InParanoid; I1RL18; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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..378
FT /note="O-methyltransferase dpfgI"
FT /id="PRO_0000451554"
FT ACT_SITE 299
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 232..233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 257
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 279..280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 295
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
SQ SEQUENCE 378 AA; 42361 MW; 673A85B13CA59958 CRC64;
MAQQAPTMQI DNLLAQVKVL GSSLNVADRA KVQKSLLDAL SHVETPYEHM LRLSGSLACI
RFGADIGLFK ALVESQEPLT CSYLGEKLNA NANILGRILR LLASARLVKQ TGLDTFTAEK
ITQELAAQAM ESGAHLLFDI HNRTYQALPD YLCENKSKDV DNMHNGIFQK AFSTDLSCYE
YLVHNPKLQG FMQDAMKLNQ TEGDWLSVLP MEDEIKRWQA SDPDRVLFVD IGGGMGHQCI
RLRGKYSDIP GRVVLQDMPI TVERIPKPMP HGIEAMPYNF EEPQPIKNAK FYYTRNVLHG
LTDSASIAAL KNVAAAMGTE SLLVIDDLII PDEGACTQAC QLDFVMMASI AGKKRTRDQW
EDKRKYNEYK CKRNSQFL
