FUS9_GIBM7
ID FUS9_GIBM7 Reviewed; 355 AA.
AC W7N6M8;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Methyltransferase FUS9 {ECO:0000303|PubMed:22652150};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:S0EHD6};
DE AltName: Full=Fusarin biosynthesis protein 9 {ECO:0000303|PubMed:22652150};
GN Name=FUS9 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_11078;
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600;
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 [2]
RP FUNCTION.
RX PubMed=17121404; DOI=10.1002/cbic.200600404;
RA Rees D.O., Bushby N., Cox R.J., Harding J.R., Simpson T.J., Willis C.L.;
RT "Synthesis of [1,2-13C2, 15N]-L-homoserine and its incorporation by the
RT PKS-NRPS system of Fusarium moniliforme into the mycotoxin fusarin C.";
RL ChemBioChem 8:46-50(2007).
RN [3]
RP FUNCTION.
RX PubMed=22652150; DOI=10.1016/j.fgb.2012.05.010;
RA Brown D.W., Butchko R.A., Busman M., Proctor R.H.;
RT "Identification of gene clusters associated with fusaric acid, fusarin, and
RT perithecial pigment production in Fusarium verticillioides.";
RL Fungal Genet. Biol. 49:521-532(2012).
CC -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC biosynthesis of the mycotoxin fusarin C (PubMed:17121404,
CC PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are
CC sufficient for fusarin production (By similarity). The roles of the
CC other FUS members are yet undetermined (By similarity). The fusarin C
CC synthetase FUS1 is responsible for the condensation of one acetyl-
CC coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage
CC of the arising heptaketide and homoserine, subsequently releasing the
CC first intermediate, prefusarin, as an alcohol with an open ring
CC structure (PubMed:17121404). The cytochrome P450 monooxygenase FUS8
CC participates in multiple oxidation processes at carbon C-20 and is able
CC to use the FUS1 product as substrate, resulting in formation of 20-
CC hydroxy-prefusarin (By similarity). This reaction seems to be essential
CC before the 2-pyrrolidone ring closure can be catalyzed by FUS2,
CC generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further
CC oxidizes carbon C-20 after ring closure, resulting in the formation of
CC carboxy-fusarin C (By similarity). As the last step, FUS9 methylates
CC the hydroxyl group at C-21 to generate fusarin C (By similarity).
CC Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and
CC fusarin A and fusarin D (By similarity). {ECO:0000250|UniProtKB:S0EHD6,
CC ECO:0000269|PubMed:17121404, ECO:0000269|PubMed:22652150}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLN8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:S0EHD6,
CC ECO:0000305|PubMed:22652150}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; DS022257; EWG52297.1; -; Genomic_DNA.
DR RefSeq; XP_018758488.1; XM_018900238.1.
DR AlphaFoldDB; W7N6M8; -.
DR SMR; W7N6M8; -.
DR EnsemblFungi; FVEG_11078T0; FVEG_11078T0; FVEG_11078.
DR GeneID; 30068614; -.
DR KEGG; fvr:FVEG_11078; -.
DR VEuPathDB; FungiDB:FVEG_11078; -.
DR eggNOG; ENOG502QQYU; Eukaryota.
DR HOGENOM; CLU_058489_0_0_1; -.
DR OMA; SWAIQWL; -.
DR OrthoDB; 689338at2759; -.
DR Proteomes; UP000009096; Chromosome 9.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..355
FT /note="Methyltransferase FUS9"
FT /id="PRO_0000437362"
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 21..25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 57..58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 84..87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 123..125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 140..142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 141..145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
SQ SEQUENCE 355 AA; 39922 MW; 756102ABA165EBC4 CRC64;
MADKSHVNNV PMQGNGAYSS HAALQHEAML KALPLFRAAA EAISKVDSTR VAIVEYGSAH
GNNSLEPMEA ILKSIHARSL ELLFSDRPEN DFCTLSKTVT EWADGLVENQ LLHPLFISMI
PRSFYQQVIP PKSAHLGFSL AALHHLDHVP QPTEDGQDES KLLQRQAHVD LATFLKLRSK
EIVSGGSLIL SFVGQASAGY ENYGGPVDAC RNAMIQMVQQ DKIPVSVAQA FRVPTYNRTL
SDVKKLMDEF TQIWKVHDLF EDDVMHPAFY ELKIQSNPSQ EASHKYAEIV IDWMMAVCSG
YFTKALQVGS QGGYTKEEEE SLLQDWVTRT KELFIRDHKD EEVICSFIYI RLERL
