ID   OMTB_ASPFN              Reviewed;         386 AA.
AC   Q9P900; B8NHY6;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Demethylsterigmatocystin 6-O-methyltransferase;
DE            EC=2.1.1.109;
DE   AltName: Full=Methyltransferase B;
GN   Name=omtB; Synonyms=AflO, dmtA; ORFNames=AFLA_139220;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=10806361; DOI=10.1016/s0378-1119(00)00126-8;
RA   Yu J., Woloshuk C.P., Bhatnagar D., Cleveland T.E.;
RT   "Cloning and characterization of avfA and omtB genes involved in aflatoxin
RT   biosynthesis in three Aspergillus species.";
RL   Gene 248:157-167(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Catalyzes both the conversion of demethylsterigmatocystin
CC       (DMST) to sterigmatocystin and the conversion of
CC       dihydrodemethylsterigmatocystin to dihydrosterigmatocystin (DHDMST)
CC       during aflatoxin biosynthesis. {ECO:0000269|PubMed:10806361}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-demethylsterigmatocystin + S-adenosyl-L-methionine = H(+) +
CC         S-adenosyl-L-homocysteine + sterigmatocystin; Xref=Rhea:RHEA:11504,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18227, ChEBI:CHEBI:18236,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.109;
CC   -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC       {ECO:0000269|PubMed:10806361}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; AF159789; AAF26223.1; -; Genomic_DNA.
DR   EMBL; EQ963478; EED51157.1; -; Genomic_DNA.
DR   RefSeq; XP_002379933.1; XM_002379892.1.
DR   AlphaFoldDB; Q9P900; -.
DR   SMR; Q9P900; -.
DR   STRING; 5059.CADAFLAP00007798; -.
DR   EnsemblFungi; EED51157; EED51157; AFLA_139220.
DR   VEuPathDB; FungiDB:AFLA_139220; -.
DR   eggNOG; KOG3178; Eukaryota.
DR   OMA; RELQVGF; -.
DR   UniPathway; UPA00287; -.
DR   PHI-base; PHI:3534; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0047145; F:demethylsterigmatocystin 6-O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:UniProtKB-UniPathway.
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   PIRSF; PIRSF005739; O-mtase; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQY0"
FT   CHAIN           2..386
FT                   /note="Demethylsterigmatocystin 6-O-methyltransferase"
FT                   /id="PRO_0000422198"
FT   REGION          177..197
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        293
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         137..150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         228..229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         273..274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         289
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
SQ   SEQUENCE   386 AA;  43161 MW;  F199017CC28DE9C1 CRC64;
     MTGLDMETIF AKIKDEYART DDVGKRQIQG HIRELQVGFY SDWDVVMRLS SGPLQVALAK
     VAIDLGIFRS LKESDTPITL AEFVKKTGAS PRLLGRILRT QAAFGLIKET GPQEYTSSAF
     TDVFANSDAA GAVVQLFDIS GPCTQILPDF LAERNYQDIT SNKDCVFQKA FGSDLTMFEW
     MPQHPKHMES LGHLMALERP VSWVDHFPIL EELGKFPAPD KVLMVDIGGG FGQQSKALRA
     KFPNLPGRLI VQDIPQTLAN AQPAAGIEFM EHNFFEPQPI QNAKFYYLRH VFHDWPDEQC
     VLILKQIIPA MGPESQILID EMVIPSTGVP WQAAFTDLLM MNSLGGVERT RAEWDDLMEQ
     AGLEIIQSKV YDSKEQAILV AVAKRT