ID   USTM_USTVR              Reviewed;         441 AA.
AC   A0A1B5L8S2;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Polyketide methyltransferase ustM {ECO:0000303|PubMed:31050129};
DE            EC=2.1.1.- {ECO:0000305|PubMed:31050129};
DE   AltName: Full=Ustilaginoidins biosynthesis cluster protein M {ECO:0000303|PubMed:31050129};
GN   Name=ustM {ECO:0000303|PubMed:31050129}; ORFNames=UVI_02036200;
OS   Ustilaginoidea virens (Rice false smut fungus) (Villosiclava virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Ustilaginoidea.
OX   NCBI_TaxID=1159556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IPU010;
RX   PubMed=27151791; DOI=10.1128/genomea.00306-16;
RA   Kumagai T., Ishii T., Terai G., Umemura M., Machida M., Asai K.;
RT   "Genome sequence of Ustilaginoidea virens IPU010, a rice pathogenic fungus
RT   causing false smut.";
RL   Genome Announc. 4:0-0(2016).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=31050129; DOI=10.1002/anie.201903759;
RA   Obermaier S., Thiele W., Fuertges L., Mueller M.;
RT   "Enantioselective phenol coupling by laccases in the biosynthesis of fungal
RT   dimeric naphthopyrones.";
RL   Angew. Chem. Int. Ed. 58:9125-9128(2019).
CC   -!- FUNCTION: Polyketide methyltransferase; part of the gene cluster that
CC       mediates the biosynthesis of ustilaginoidins, dimeric gamma-
CC       naphthopyrones isolated from different fungal species
CC       (PubMed:31050129). The first step in the biosynthesis of
CC       ustilaginoidins is the production of gamma-naphthopyrone precursor YWA1
CC       by the non-reducing polyketide synthase ustP, via condensation of one
CC       acetyl-CoA starter unit with 6 malonyl-CoA units (PubMed:31050129).
CC       YWA1 is then probably substrate of the ustZ to yield norrubrofusarin
CC       via a dehydration reaction (Probable). A key enzyme in the biosynthetic
CC       pathway is the laccase ustL, which catalyzes the oxidative dimerization
CC       of norrubrofusarin to ustilaginoidin A (PubMed:31050129). It can
CC       produce the M- and P-atropisomers in varying amounts, depending on the
CC       reaction conditions (PubMed:31050129). For the biosynthesis of 3-
CC       methylustilaginoid in derivatives such as chaetochromin A, a methylated
CC       derivative of YWA1 is required (Probable). The C-methylation is
CC       considered to be catalyzed by ustM, the phosphopantetheine attachment
CC       site of which indicates that it acts on the growing polyketide chain
CC       before release of the product (Probable). For the biosynthesis of
CC       chaetochromin A, it is assumed that saturation of the D2 double bond
CC       takes place before dimerization, and is probably catalyzed by an
CC       external reductase because no candidate gene was identified within the
CC       cluster (Probable). {ECO:0000269|PubMed:31050129,
CC       ECO:0000305|PubMed:31050129}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:31050129}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; BBTG02000019; GAO19029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B5L8S2; -.
DR   SMR; A0A1B5L8S2; -.
DR   Proteomes; UP000054053; 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; IPR041068; HTH_51.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF18558; HTH_51; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Transferase.
FT   CHAIN           1..441
FT                   /note="Polyketide methyltransferase ustM"
FT                   /id="PRO_0000448924"
FT   REGION          266..368
FT                   /note="Methyltransferase (CMeT) domain"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   441 AA;  48781 MW;  4254C67336C53D07 CRC64;
     MDMLQFFRDA LVQETGRHVD NDDFDALFSE LGADPLVGVA VIERVTNKTV EKAPRAARPP
     REAPLPRGNV RNAFQDACSH VQEFLRKAGS ANFWSRVYPA QRQLVLAFVN DAFDRLGCSL
     ADMPVGTIVT YPRGVLDKHR RVFDGAIFEI LADGGLVNVD PELGAIRTST VVDKTPPQQI
     LATIILEHPQ FANLHRLLNV TGSQFAECLT GRLDPIKLLF GRSKDLLQDF YTNAPMSLAA
     SLHLVAVIKR LLADGEYRPG KSIDILEVGA GLGGTTRFVV EALIEAQVPF RYVYTDISAS
     FFAASKNRYK SLPPGSSMEF LVLDVEIPPP ETLLGGFDVV VSTNCIHATR NLGVSCSNVR
     KLLRGGGFFA LIEFTSRMYW LDLVFGLLDG WWLFEDGRKH CTVDETVWEE KLQLSGFSDV
     LWADVEGDDK SSLQLLVACT D