ID   DESB_ASPDE              Reviewed;         419 AA.
AC   A0A0N9HN32;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=O-methyltransferase desB {ECO:0000303|PubMed:26389790};
DE            EC=2.1.1.- {ECO:0000305|PubMed:26389790};
DE   AltName: Full=Desertorin biosynthesis cluster protein B {ECO:0000303|PubMed:26389790};
GN   Name=desB {ECO:0000303|PubMed:26389790};
GN   ORFNames=EMD_0003 {ECO:0000303|PubMed:26389790};
OS   Aspergillus desertorum (Emericella desertorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1810909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=CBS 653.73 / NBRC 30840;
RX   PubMed=26389790; DOI=10.1021/jacs.5b06776;
RA   Mazzaferro L.S., Huettel W., Fries A., Mueller M.;
RT   "Cytochrome P450-catalyzed regio- and stereoselective phenol coupling of
RT   fungal natural products.";
RL   J. Am. Chem. Soc. 137:12289-12295(2015).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of the bicoumarin desertorin
CC       (PubMed:26389790). The non-reducing polyketide synthase desS first
CC       catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-
CC       methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A
CC       molecules (PubMed:26389790). Further O-methylation by desB leads to the
CC       formation of 7-demethylsiderin (PubMed:26389790). Then, an oxidative
CC       phenol coupling catalyzed by the cytochrome P450 monooxygenase desC
CC       forms the 6,8'-dimer M-desertorin A via dimerization the monomeric
CC       precursor, 7-demethylsiderin (PubMed:26389790). M-desertorin A is
CC       further converted to M-desertorin C (PubMed:26389790).
CC       {ECO:0000269|PubMed:26389790}.
CC   -!- COFACTOR:
CC       Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:26389790}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; KT583602; ALG03238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N9HN32; -.
DR   SMR; A0A0N9HN32; -.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..419
FT                   /note="O-methyltransferase desB"
FT                   /id="PRO_0000442167"
FT   ACT_SITE        326
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         255..256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         306..307
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         323
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   419 AA;  46180 MW;  37C023B242D93CC6 CRC64;
     MGTETEYLQS IQQALKSLTT AANNCQLTYT HAVGQDVHSL CAREAVRKTL VLEAYKFLQI
     AQGPVDAAVT CFEQTAHLAS VRALLEAGVF EVLPTDGTPR TMKEVAEKLD VDESLLARLM
     RHASLYGPLE ETGPGSYRHT PFSLVYLRPE IRGMVRFAMD EHMPAHLKLH EYLQQTSWTA
     PSSSTNNPYT HAHSITGTSM FANLSAPSNK HRLDAFNDAM TVQATTAIWM IDLFPFHEVL
     SPSASADTVL AVDIGGGTGR AISRIRSLAG NLPGRYILQD QAHVISNLPS PSPSSYLDGI
     ETMTHDFFTP QPVAGAQIYL IRRCLHNWPE ESVIRILRNI VPAMARTNSR LLIEEIIVPE
     SNSGIEEGWM DMIMMALGAK QRTLEEWKGV LGTAGLEVVT VYRVDGICHG LIEARVKSE