LUC1_FUSSX
ID LUC1_FUSSX Reviewed; 361 AA.
AC A0A6J4B4P7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Methyltransferase LUC1 {ECO:0000303|PubMed:32043422};
DE EC=2.1.1.- {ECO:0000269|PubMed:32043422};
DE AltName: Full=Lucilactaene biosynthesis cluster protein 1 {ECO:0000303|PubMed:32043422};
GN Name=LUC1 {ECO:0000303|PubMed:32043422};
OS Fusarium sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=29916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=RK97-94;
RX PubMed=32043422; DOI=10.1080/09168451.2020.1725419;
RA Kato S., Motoyama T., Futamura Y., Uramoto M., Nogawa T., Hayashi T.,
RA Hirota H., Tanaka A., Takahashi-Ando N., Kamakura T., Osada H.;
RT "Biosynthetic gene cluster identification and biological activity of
RT lucilactaene from Fusarium sp. RK97-94.";
RL Biosci. Biotechnol. Biochem. 84:1303-1307(2020).
CC -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC biosynthesis of the mycotoxin lucilactaene and the lucilactaene-related
CC compound NG-391 that act as cell cycle inhibitors with potent growth
CC inhibitory activity against malarial parasites, moderate growth
CC inhibitory activity against cancer cells, and no activity against
CC bacteria and fungi (PubMed:32043422). Within the cluster, LUC5, LUC6,
CC LUC2 and LUC1 are sufficient for lucilactaene production (By
CC similarity). The roles of the other LUC members are yet undetermined
CC (By similarity). The hybrid PKS-NRPS synthetase LUC5 is responsible for
CC the condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-
CC CoA units and the amide linkage of the arising heptaketide and
CC homoserine, subsequently releasing the first intermediate, as an
CC alcohol with an open ring structure (By similarity). Lucilactaene and
CC NG-391 lack the 7-methyl group present in fusarins which is inserted in
CC fusarins by the C-methyltransferase (CMeT) domain of the fusarin
CC synthetase FUS1, suggesting that the CMet domain of LUC5 does not
CC methylate this position (Probable). The cytochrome P450 monooxygenase
CC LUC2 participates in multiple oxidation processes at carbon C-20 and is
CC able to use the LUC5 product as substrate (By similarity). This
CC reaction seems to be essential before the 2-pyrrolidone ring closure
CC can be catalyzed by LUC6 (By similarity). LUC2 is able to further
CC oxidizes carbon C-20 after ring closure, resulting in the formation of
CC demethyllucilactaene (By similarity). As the last step, the
CC methyltransferase LUC1 methylates the hydroxyl group at C-21 to
CC generate lucilactaene (PubMed:32043422). {ECO:0000250|UniProtKB:S0EHD6,
CC ECO:0000269|PubMed:32043422, ECO:0000305|PubMed:32043422}.
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:32043422}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of lucilactaene and NG-
CC 391, and leads to the accumulation of demethyllucilactaene and (8Z)-
CC demethyllucilactaene. {ECO:0000269|PubMed:32043422}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; LC515193; BBQ09592.1; -; Genomic_DNA.
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; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..361
FT /note="Methyltransferase LUC1"
FT /id="PRO_0000454633"
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 60..61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 87..90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 126..128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 143..145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 144..148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
SQ SEQUENCE 361 AA; 40263 MW; 4B22A9E8FC7E6BAC CRC64;
MADTAHINDV PMQGKGLYSS HAALQHEAML KALPLLQQAT NTVVTNVNRN LRPLTVVEYG
SAHGNNSIQP MVTILDSTPP GDIQLVFSDR PENDFNTLST TVTTWAEGLD KAKFPHSIFP
AMIPRSFYRQ VVPSRSADLG FSLAALHHLD HVPKSQDGVD HQALLKRQAH LDLLQFLKLR
ADEIVPGGSL VLSFVSQSSS GRENYAGLVD ACRNAMIDMV KDGTLPGAVA GSFYVPTYNR
TLQDVQKVIE EVIPTWIAHE VFEQDCLHPA KKDLELQKSS DDYDSDEASR RYADVVVDWL
MAVCAGYFLK AVKVGSDNTF TGEDAEKFLA DWVKRTKHFF YKDHRDEDVV CSFIFVRLER
V
