ID   USTE_USTVR              Reviewed;         284 AA.
AC   A0A1B5L6A5;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Probable O-methyltransferase ustE {ECO:0000303|PubMed:31050129};
DE            EC=2.1.1.- {ECO:0000305};
DE   AltName: Full=Ustilaginoidins biosynthesis cluster protein E {ECO:0000303|PubMed:31050129};
GN   Name=ustE {ECO:0000303|PubMed:31050129}; ORFNames=UVI_02036190;
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.
RC   STRAIN=IPU010;
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: Probable O-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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC       superfamily. Isoprenylcysteine carboxyl methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BBTG02000019; GAO19109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B5L6A5; -.
DR   Proteomes; UP000054053; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR   InterPro; IPR010721; DUF1295.
DR   Pfam; PF06966; DUF1295; 1.
DR   PROSITE; PS50244; S5A_REDUCTASE; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..284
FT                   /note="Probable O-methyltransferase ustE"
FT                   /id="PRO_0000448925"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   284 AA;  31284 MW;  ABE3E94CBCAD10BE CRC64;
     MADAKAVAKA ELKSKDFVPR GNKSSSPLNT TLYLGLRALD CYIQYLILSR ATGSFIIKFF
     GGSIIPHGPP VEAGFMHIEK LGLSGYRLLL LFMDILAAAK HFWFVLTVAE EAWTLTGAIV
     VGLDNIFFDT LNNLLFLCAA TSAASSKAGG ETLANPYLAT GFIIFAVGLV TECVCEIDRK
     VFKKNPMNKG KPYTGGLFSL VRHPNYTAFT IWRSGLALAS GGMIYGMSIA MFFMWDFSNR
     AVPALDEYCT KRVSYGPRDS TSTNWSRIWL LMTSSLVRRY VGRV