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DPFGB_GIBZE
ID   DPFGB_GIBZE             Reviewed;         242 AA.
AC   P9WEY0; A0A098DL10; A0A0E0S804;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Terpene cyclase dpfgB {ECO:0000303|PubMed:32286350};
DE            EC=4.2.3.- {ECO:0000305|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein B {ECO:0000303|PubMed:32286350};
GN   Name=dpfgB {ECO:0000303|PubMed:32286350};
GN   ORFNames=FG04594, FGRAMPH1_01T15659;
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: Terpene cyclase; part of the gene cluster that mediates the
CC       biosynthesis of diterpenoid pyrones (PubMed:32286350). The first step
CC       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: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 paxB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CEF79629.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: dpfgB and dpfgG.; Evidence={ECO:0000305};
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DR   EMBL; HG970333; CEF79629.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P9WEY0; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000070720; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR039020; PaxB-like.
DR   PANTHER; PTHR42038; PTHR42038; 1.
PE   1: Evidence at protein level;
KW   Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..242
FT                   /note="Terpene cyclase dpfgB"
FT                   /id="PRO_0000451529"
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   242 AA;  27585 MW;  E801059E721AC120 CRC64;
     MEVADPSRAP PEYKDVAWIA DTCKLLMGIG WTTNYVGMIY KSLKDETYAM ALMALCCNFA
     WELTYALIYP FGSDLEMYVH FSGLMLNCGV MYTAVKNAHR EWGHSPLVLR NLPLIFIICV
     SGFMSGHVAL AAQVGPSLAQ AWSAYGCQLL LSVGGLCQLL CRGHSRGASY FLWFSRFFGS
     LVLVPQDILR YKYWRVDHEY MGSPLYIWFV CIFLLLDGSY GICLWYVRRF ERQTAVAHKK
     KK
 
 
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