ID   MT1_BEAB2               Reviewed;         249 AA.
AC   J4KLK4;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Methyltransferase 1 {ECO:0000303|PubMed:34903054};
DE            Short=MT1 {ECO:0000303|PubMed:34903054};
DE            EC=2.1.1.- {ECO:0000269|PubMed:34903054};
DE   AltName: Full=Sordarin/hypoxysordarin biosynthesis cluster protein D {ECO:0000303|PubMed:34903054};
GN   ORFNames=BBA_08685;
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860;
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA   St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX   PubMed=34903054; DOI=10.1128/mbio.03279-21;
RA   Chen B., Sun Y., Li S., Yin Y., Wang C.;
RT   "Inductive production of the iron-chelating 2-pyridones benefits the
RT   producing fungus to compete for diverse niches.";
RL   MBio 12:e0327921-e0327921(2021).
CC   -!- FUNCTION: Methyltransferase; part of the pathway that mediates the
CC       biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds
CC       involved in iron stress tolerance, competition with the natural
CC       competitor fungus Metarhizium robertsii and insect hosts infection
CC       (PubMed:34903054). Methylates pyridovericin-N-O-(beta-D-
CC       glucopyranoside) produced by the UDP-glucosyltransferase GT1 to yield
CC       pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP)
CC       (PubMed:34903054). The pathway begins with the assembly of the
CC       polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the
CC       help of the enoyl reductase tenC. These enzymes catalyze the synthesis
CC       of the pyrrolidine-2-dione intermediates pretellinin A, 11-
CC       hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-
CC       hydropretellenin A, 12-oxopretellenin A and prototellinin D. The
CC       cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring
CC       expansion of pretenellin A and 14-hydropretellenin A to form the 2-
CC       pyridone core, leading to pretenellin B and pyridovericin,
CC       respectively. The cytochrome P450 monooxygenase tenB is then required
CC       for the selective N-hydroxylation of the 2-pyridone nitrogen of yield
CC       tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-
CC       glucosyltransferase GT1 and the methyltransferase MT1, located outside
CC       the tenS gene cluster, contribute to the stepwise glycosylation and
CC       methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-
CC       methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds
CC       such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A
CC       are also produced but the enzymes involved in their biosynthesis have
CC       still to be determined (PubMed:34903054).
CC       {ECO:0000269|PubMed:34903054}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:34903054}.
CC   -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC       transcription factor tenR and is induced during cocultures with the
CC       natural competitor fungus Metarhizium robertsii.
CC       {ECO:0000269|PubMed:34903054}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of detectable
CC       pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP).
CC       {ECO:0000269|PubMed:34903054}.
CC   -!- SIMILARITY: Belongs to the FkbM methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; JH725187; EJP62359.1; -; Genomic_DNA.
DR   RefSeq; XP_008602004.1; XM_008603782.1.
DR   EnsemblFungi; EJP62359; EJP62359; BBA_08685.
DR   GeneID; 19891697; -.
DR   HOGENOM; CLU_063680_0_0_1; -.
DR   InParanoid; J4KLK4; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR006342; FkbM_mtfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF05050; Methyltransf_21; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR01444; fkbM_fam; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..249
FT                   /note="Methyltransferase 1"
FT                   /id="PRO_0000455691"
SQ   SEQUENCE   249 AA;  28021 MW;  9F9DD0D2091CA10A CRC64;
     MALVEKIQLT DDFSVYANPA AKLEVEFIHK EIFIDKCYDV APFPDDSFIV DAGGNIGMFT
     LYMKRKYPQS TILAFEPAPA TFSTFQRNME LHNVSGVQAH QCGLGREDAS LALTFYPQMP
     GNSTLYAEDK TNQMKSVDQN HPIAKLMQET HEVQVDVKRL SDFLGEVPNL KRVNLLKVDV
     EGAEMDVLRG LDDEHWDLID NVVVELCDSK GDFATAKTLL ESKGFAVAVE RPDWAPPDLK
     MYMLIAKRN