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FSL2_GIBZE
ID   FSL2_GIBZE              Reviewed;         248 AA.
AC   I1S165;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Thioesterase FSL2 {ECO:0000303|PubMed:22252016};
DE            EC=3.1.2.- {ECO:0000305|PubMed:27983606};
DE   AltName: Full=Fusarielin biosynthesis cluster protein 2 {ECO:0000303|PubMed:22252016};
GN   Name=FSL2 {ECO:0000303|PubMed:22252016};
GN   ORFNames=FG10463, FGRAMPH1_01T08163;
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   INDUCTION, AND FUNCTION.
RX   PubMed=22252016; DOI=10.1111/j.1462-2920.2011.02696.x;
RA   Soerensen J.L., Hansen F.T., Sondergaard T.E., Staerk D., Lee T.V.,
RA   Wimmer R., Klitgaard L.G., Purup S., Giese H., Frandsen R.J.;
RT   "Production of novel fusarielins by ectopic activation of the polyketide
RT   synthase 9 cluster in Fusarium graminearum.";
RL   Environ. Microbiol. 14:1159-1170(2012).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=27983606; DOI=10.3390/molecules21121710;
RA   Droce A., Saei W., Joergensen S.H., Wimmer R., Giese H., Wollenberg R.D.,
RA   Sondergaard T.E., Soerensen J.L.;
RT   "Functional Analysis of the Fusarielin Biosynthetic Gene Cluster.";
RL   Molecules 21:0-0(2016).
CC   -!- FUNCTION: Thioesterase; part of the gene cluster that mediates the
CC       biosynthesis of fusarielins F, G and H, decaketide compounds with 5
CC       methylations and a decaline core that act as mycoestrogens as they
CC       stimulate growth of MCF-7 breast cancer cells (PubMed:22252016,
CC       PubMed:27983606). The initial compound in the pathway is produced by
CC       the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl
CC       reductase (ER) domain and biosynthesis of fusarielins relies on the
CC       trans-acting enoyl reductase FSL5, before it is released through
CC       hydrolysis catalyzed by the thioesterase FSL2 (PubMed:22252016,
CC       PubMed:27983606). Fusarielins F, G, and H have a C11=C12 cis double
CC       bond and is fully reduced between C10 and C11 and between C12 and C13.
CC       FSL3 can be involved in the formation of the C11=C12 cis double bond by
CC       moving a hypothetical C10=C11 or C12=C13 trans double bond to form
CC       prefusarielin (PubMed:27983606). Prefusarielin is oxygenated at C15 and
CC       C16 by the cytochrome P450 monooxygenase FSL4, resulting in fusarielin
CC       F, which subsequently is epoxidized into fusarielin G by the same
CC       enzyme (PubMed:27983606). The final step in the pathway is a reduction
CC       of the carboxylic acid moiety to yield fusarielin H via a still
CC       undetermined mechanism (PubMed:27983606). {ECO:0000269|PubMed:22252016,
CC       ECO:0000269|PubMed:27983606}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:27983606}.
CC   -!- INDUCTION: Expression is positively regulated by the fusarielin
CC       biosynthesis cluster-specific transcription factor FSL7, probably via
CC       its binding at the 5'-CGGNNNCCG-3' motif present in the promoter of all
CC       the cluster genes. {ECO:0000269|PubMed:22252016}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of fusarielins F, G and
CC       H. {ECO:0000269|PubMed:27983606}.
CC   -!- SIMILARITY: Belongs to the LovG family. {ECO:0000305}.
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DR   EMBL; HG970332; CEF75885.1; -; Genomic_DNA.
DR   RefSeq; XP_011319442.1; XM_011321140.1.
DR   AlphaFoldDB; I1S165; -.
DR   SMR; I1S165; -.
DR   GeneID; 23557368; -.
DR   KEGG; fgr:FGSG_10463; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G08163; -.
DR   eggNOG; KOG2551; Eukaryota.
DR   HOGENOM; CLU_051938_0_1_1; -.
DR   InParanoid; I1S165; -.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR005645; FSH_dom.
DR   Pfam; PF03959; FSH1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..248
FT                   /note="Thioesterase FSL2"
FT                   /id="PRO_0000444960"
FT   ACT_SITE        125
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
FT   ACT_SITE        195
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
FT   ACT_SITE        223
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
SQ   SEQUENCE   248 AA;  27075 MW;  2AA15C3B01BF04F0 CRC64;
     MTIQSTANHQ DGYLPAILCL HGAGTNATIF NLQARTIVRC LKHKFRFIFV NAPFESLPGP
     GVIPTFAEIR PYLRWHCDEN AIQEFDVSPE LVDNERRLVR SMISDKIEQE ATGPSLGIVG
     VMAFSQGTRV ATGLCLDPEF GSSIQFAIII AGTFPALSLE NPVSDSETTN LFSGINGNKH
     EQLQIPSVHV QGTMDPWGPE SARLLKECWS ADLAMVVKFH GAHQVPTSKK DAQAVAQAVL
     SCWDSAQT
 
 
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