FSL5_GIBZE
ID FSL5_GIBZE Reviewed; 359 AA.
AC A0A0E0RXA7;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Trans-enoyl reductase FSL5 {ECO:0000303|PubMed:22252016};
DE EC=1.-.-.- {ECO:0000305|PubMed:27983606};
DE AltName: Full=Fusarielin biosynthesis cluster protein 5 {ECO:0000303|PubMed:22252016};
GN Name=FSL5 {ECO:0000303|PubMed:22252016};
GN ORFNames=FG10460, FGRAMPH1_01T08157;
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: Trans-enoyl reductase; part of the gene cluster that mediates
CC the 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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
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 zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; HG970332; CEF75882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E0RXA7; -.
DR SMR; A0A0E0RXA7; -.
DR STRING; 5518.FGSG_10460P0; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G08157; -.
DR eggNOG; KOG1198; Eukaryota.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..359
FT /note="Trans-enoyl reductase FSL5"
FT /id="PRO_0000444963"
FT BINDING 47..50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 134..141
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 169..172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 192..195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 210
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 257..258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 277..281
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 346..347
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 359 AA; 38517 MW; ED5997606895DE00 CRC64;
MTNLPSHHTA IVGSEDGSLK VAEQVPLPRL ENDMILVRNT AVALNPIDGK MVGNLASVGA
VAGMDYVGTV VGIGPKVKTA SEIQLGDRVC GAVQGMHSLT PSVGAFAQFV GATDIVTLKV
PPSMTVEDAA TLGSGVGTIG LALFRSLDVP GYPEAPATER IPVLVYGGST ATGTLAIQLL
KLSGLIPITT CSPHNFDLVK SFGAEAVFDY RRPETPDEIR KFTRNSLKYV LDCISEPETM
QFCYKCIGRT GGKYTALEPF PQFLHTRPTI QPDWVLGPTL LGKPIGWGPP FERVGDPDVR
EFAIKWFATA QRLLDQGKLQ THPVKLMEGG FEGILCGLEM LKKKQVSGQK LVYMIPQVA
