DPFGC_GIBZE
ID DPFGC_GIBZE Reviewed; 330 AA.
AC I1RL16;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Polyprenyl transferase dpfgC {ECO:0000303|PubMed:32286350};
DE EC=2.5.1.- {ECO:0000305|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein C {ECO:0000303|PubMed:32286350};
GN Name=dpfgC {ECO:0000303|PubMed:32286350};
GN ORFNames=FG04593, FGRAMPH1_01T15657;
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, 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: Polyprenyl transferase; part of the gene cluster that
CC mediates the biosynthesis of diterpenoid pyrones (PubMed:32286350). The
CC first step of the pathway is the synthesis of the alpha-pyrone moiety
CC by the polyketide synthase dpfgA via condensation of one acetyl-CoA
CC starter unit with 3 malonyl-CoA units and 2 methylations (Probable).
CC The alpha-pyrone is then combined with geranylgeranyl pyrophosphate
CC (GGPP) formed by the GGPP synthase dpfgD through the action of the
CC prenyltransferase dpfgC to yield a linear alpha-pyrone diterpenoid
CC (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic
CC pathway involve the decalin core formation, which is initiated by the
CC epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase
CC dpfgE, and is followed by a cyclization cascade catalyzed by the
CC terpene cyclase dpfgB (Probable). The short chain
CC dehydrogenase/reductase dpfgG then oxidizes the 8S hydroxy group to a
CC ketone and the short chain dehydrogenase/reductase dpfgH reduces the
CC ketone to the 8R hydroxy group to yield higginsianin B
CC (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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P32378};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:32286350}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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 UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; HG970333; CEF79628.1; -; Genomic_DNA.
DR RefSeq; XP_011320988.1; XM_011322686.1.
DR AlphaFoldDB; I1RL16; -.
DR SMR; I1RL16; -.
DR STRING; 5518.FGSG_04593P0; -.
DR GeneID; 23551832; -.
DR KEGG; fgr:FGSG_04593; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G15657; -.
DR eggNOG; KOG1381; Eukaryota.
DR HOGENOM; CLU_075330_0_0_1; -.
DR InParanoid; I1RL16; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 3.
DR Pfam; PF01040; UbiA; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..330
FT /note="Polyprenyl transferase dpfgC"
FT /id="PRO_0000451534"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 330 AA; 37185 MW; E409CE7BCFF3EBA3 CRC64;
MSRQTDMDPG TYVPDIGGLR FWDMWKEVVF VFVNDTKQKH GGGSETGAGA FFPQYSKYPA
MAARSKTKFL GELLILSRFH KYNPVFTTFA GDRTISTAFV FQQTALCVLA AYLFCGAGMV
WNDWIDRDID AKVARTKHRP LAMGSVTTTE AMVWMTLQVI MSWGVLRVML DNKDVLKHLI
PVMVASVLYP FGKRYLARKL MIYPQYILAF TIAWPAIPGR AAICGRHESF TETTRQCLPL
CIMVFFWTIY LNTAYSYQDV VDDRKLKVNS FYNIAGNHIH VLLVLLVSPI ILAQFDPKQP
ASGGTLHKSN FILGVWTILA CAAEVFLTSA
