FUS9_GIBF5
ID FUS9_GIBF5 Reviewed; 355 AA.
AC S0EHD6;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Methyltransferase FUS9 {ECO:0000303|PubMed:23932525};
DE EC=2.1.1.- {ECO:0000305|PubMed:23932525};
DE AltName: Full=Fusarin biosynthesis protein 9 {ECO:0000303|PubMed:23932525};
GN Name=FUS9 {ECO:0000303|PubMed:23932525}; ORFNames=FFUJ_10050;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [2]
RP INDUCTION.
RX PubMed=20572938; DOI=10.1111/j.1365-2958.2010.07263.x;
RA Wiemann P., Brown D.W., Kleigrewe K., Bok J.W., Keller N.P., Humpf H.U.,
RA Tudzynski B.;
RT "FfVel1 and FfLae1, components of a velvet-like complex in Fusarium
RT fujikuroi, affect differentiation, secondary metabolism and virulence.";
RL Mol. Microbiol. 77:972-994(2010).
RN [3]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=23932525; DOI=10.1016/j.chembiol.2013.07.004;
RA Niehaus E.M., Kleigrewe K., Wiemann P., Studt L., Sieber C.M.,
RA Connolly L.R., Freitag M., Gueldener U., Tudzynski B., Humpf H.U.;
RT "Genetic manipulation of the Fusarium fujikuroi fusarin gene cluster yields
RT insight into the complex regulation and fusarin biosynthetic pathway.";
RL Chem. Biol. 20:1055-1066(2013).
CC -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC biosynthesis of the mycotoxin fusarin C (PubMed:23932525). Within the
CC cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin
CC production (PubMed:23932525). The roles of the other FUS members are
CC yet undetermined (PubMed:23932525). The fusarin C synthetase FUS1 is
CC responsible for the condensation of one acetyl-coenzyme A (CoA) unit
CC with six malonyl-CoA units and the amide linkage of the arising
CC heptaketide and homoserine, subsequently releasing the first
CC intermediate, prefusarin, as an alcohol with an open ring structure
CC (PubMed:23932525). The cytochrome P450 monooxygenase FUS8 participates
CC in multiple oxidation processes at carbon C-20 and is able to use the
CC FUS1 product as substrate, resulting in formation of 20-hydroxy-
CC prefusarin (PubMed:23932525). This reaction seems to be essential
CC before the 2-pyrrolidone ring closure can be catalyzed by FUS2,
CC generating 20-hydroxy-fusarin (PubMed:23932525). FUS8 is able to
CC further oxidizes carbon C-20 after ring closure, resulting in the
CC formation of carboxy-fusarin C (PubMed:23932525). As the last step,
CC FUS9 methylates the hydroxyl group at C-21 to generate fusarin C
CC (PubMed:23932525). Fusarin C can then rearrange to epi-fusarin C, the
CC (z)-isomers, and fusarin A and fusarin D (PubMed:23932525).
CC {ECO:0000269|PubMed:23932525}.
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:0000269|PubMed:23932525}.
CC -!- INDUCTION: Expressed under high amounts of nitrogen via regulation by
CC GLN1 (PubMed:23932525). Moreover, components of the fungal-specific
CC velvet complex VEL1, VEL2 and LAE1 act also as positive regulators of
CC expression (PubMed:20572938, PubMed:23932525). Finally, expression is
CC induced under acidic conditions in a PACC-independent manner
CC (PubMed:23932525). {ECO:0000269|PubMed:20572938,
CC ECO:0000269|PubMed:23932525}.
CC -!- DISRUPTION PHENOTYPE: Accumulates carboxy-fusarins (PubMed:23932525).
CC {ECO:0000269|PubMed:23932525}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; HF679031; CCT73267.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EHD6; -.
DR SMR; S0EHD6; -.
DR EnsemblFungi; CCT73267; CCT73267; FFUJ_10050.
DR VEuPathDB; FungiDB:FFUJ_10050; -.
DR HOGENOM; CLU_058489_0_0_1; -.
DR BioCyc; MetaCyc:MON-19360; -.
DR Proteomes; UP000016800; 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 1: Evidence at protein level;
KW Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..355
FT /note="Methyltransferase FUS9"
FT /id="PRO_0000437361"
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; 39638 MW; 3E595BA269E8621B CRC64;
MADKSHVNNV PMQGNGAYSS HAALQHEAML KALPLFQAAA EVIANVDSTR ISIVEYGSAH
GNNSLEPMEA ILKSIPTESL ELLFSDRPEN DFCTLSKTVT AWADGIVGNQ LLNPLFISMI
PRSFYQQVVP PKSAHLGFSL AALHHLDHVP QPTEDGQDES ELLQQQAHVD LATFLKLRSQ
EIVSGGSLIL SFVSQASAGY ENYSGPVDAC RNAMIEMVQQ GKIPLSVAQA FRVPTYNRTL
SDVKKVMDEF TQTWKVHDLF EDDVMHPAFH KLKIQSNPSL EASHKYAEVV IDWMMAVCSG
YFTKALQVGS QGGYTKQEEE GLLQVWVTRT KEFFIRDYKD KEVICSFIYI RLERL
