ID   SIRN_LEPMC              Reviewed;         284 AA.
AC   Q6Q870;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 2.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=N-methyltransferase sirN {ECO:0000303|PubMed:15387811};
DE            EC=2.1.1.- {ECO:0000305|PubMed:15387811};
DE   AltName: Full=Sirodesmin biosynthesis protein N {ECO:0000303|PubMed:15387811};
GN   Name=sirN {ECO:0000303|PubMed:15387811};
OS   Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=5022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=15387811; DOI=10.1111/j.1365-2958.2004.04215.x;
RA   Gardiner D.M., Cozijnsen A.J., Wilson L.M., Pedras M.S., Howlett B.J.;
RT   "The sirodesmin biosynthetic gene cluster of the plant pathogenic fungus
RT   Leptosphaeria maculans.";
RL   Mol. Microbiol. 53:1307-1318(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=18272357; DOI=10.1016/j.mycres.2007.08.017;
RA   Fox E.M., Howlett B.J.;
RT   "Biosynthetic gene clusters for epipolythiodioxopiperazines in filamentous
RT   fungi.";
RL   Mycol. Res. 112:162-169(2008).
RN   [3]
RP   FUNCTION.
RX   PubMed=19762440; DOI=10.1099/mic.0.033886-0;
RA   Kremer A., Li S.M.;
RT   "A tyrosine O-prenyltransferase catalyses the first pathway-specific step
RT   in the biosynthesis of sirodesmin PL.";
RL   Microbiology 156:278-286(2010).
RN   [4]
RP   FUNCTION.
RX   PubMed=21038099; DOI=10.1007/s00253-010-2956-x;
RA   Zou H.X., Xie X., Zheng X.D., Li S.M.;
RT   "The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-
RT   prenylations.";
RL   Appl. Microbiol. Biotechnol. 89:1443-1451(2011).
RN   [5]
RP   FUNCTION.
RX   PubMed=24083562; DOI=10.1021/cb400691z;
RA   Rudolf J.D., Poulter C.D.;
RT   "Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on
RT   tyrosine and tryptophan derivatives.";
RL   ACS Chem. Biol. 8:2707-2714(2013).
RN   [6]
RP   FUNCTION.
RX   PubMed=27390873; DOI=10.1371/journal.pone.0158945;
RA   Dopstadt J., Neubauer L., Tudzynski P., Humpf H.U.;
RT   "The epipolythiodiketopiperazine gene cluster in Claviceps purpurea:
RT   dysfunctional cytochrome P450 enzyme prevents formation of the previously
RT   unknown clapurines.";
RL   PLoS ONE 11:E0158945-E0158945(2016).
CC   -!- FUNCTION: N-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP)
CC       characterized by a disulfide bridged cyclic dipeptide and that acts as
CC       a phytotoxin which is involved in the blackleg didease of canola
CC       (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD catalyzes the
CC       O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl
CC       diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore
CC       represents probably the first pathway-specific enzyme in the
CC       biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099,
CC       PubMed:24083562). 4-O-dimethylallyl-L-Tyr, then undergoes condensation
CC       with L-Ser in a reaction catalyzed by the non-ribosomal peptide
CC       synthase sirP to form the diketopiperazine (DKP) backbone
CC       (PubMed:18272357). Further bishydroxylation of the DKP performed by the
CC       cytochrome P450 monooxygenase sirC leads to the production of the
CC       intermediate phomamide (PubMed:27390873). This step is essential to
CC       form the reactive thiol group required for toxicity of sirodesmin PL
CC       (PubMed:27390873). The next steps of sirodesmin biosynthesis are not
CC       well understood yet but some predictions could be made from
CC       intermediate compounds identification (PubMed:18272357). Phomamide is
CC       converted into phomalizarine via oxidation, probably by sirT
CC       (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and
CC       reduction steps convert phomalizarine to deacetyl sirodesmin
CC       (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates
CC       deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357).
CC       {ECO:0000269|PubMed:19762440, ECO:0000269|PubMed:21038099,
CC       ECO:0000269|PubMed:24083562, ECO:0000269|PubMed:27390873,
CC       ECO:0000305|PubMed:15387811, ECO:0000305|PubMed:18272357}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:15387811}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT01502.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY553235; AAT01502.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q6Q870; -.
DR   SMR; Q6Q870; -.
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; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase; Virulence.
FT   CHAIN           1..284
FT                   /note="N-methyltransferase sirN"
FT                   /id="PRO_0000437730"
SQ   SEQUENCE   284 AA;  31514 MW;  9076ECED596B2528 CRC64;
     MTVETKDLPE SNYLLDYDDT EKRRLREQHD LIKAYTGKLI LAPLDLTKPN LKILDSGTFD
     GHWLTEAAKP LTTPLLTGTD ISPAAFPNPP PQNTSFHIQS ITDPWPASWQ NTFDLVHQRL
     VLAGTTPTGG LDAVRNLAGL AKPGGWVQLI EGKLLAESQR TRFPALHRFH SFIERMLPGF
     GWNIRAGLMV GGWLGEVGLE EVGEMEVEIP VGRANGDGRL GAMAEKNLRD VMGVWRQASS
     KLPADSPFKA SELEEIFVDW DKEIETIGSL LRFAVVWGRR PALD