ID   OPAF_ASPUT              Reviewed;         420 AA.
AC   A0A0C1E5J2;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=O-methyltransferase opaF {ECO:0000303|PubMed:33004788};
DE            EC=2.1.1.- {ECO:0000269|PubMed:33004788};
DE   AltName: Full=Oxepinamide F biosynthesis cluster protein F {ECO:0000303|PubMed:33004788};
GN   Name=opaF {ECO:0000303|PubMed:33004788}; ORFNames=HK57_00060;
OS   Aspergillus ustus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=40382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC   STRAIN=3.3904;
RX   PubMed=25706180; DOI=10.1371/journal.pone.0116089;
RA   Pi B., Yu D., Dai F., Song X., Zhu C., Li H., Yu Y.;
RT   "A genomics based discovery of secondary metabolite biosynthetic gene
RT   clusters in Aspergillus ustus.";
RL   PLoS ONE 10:e0116089-e0116089(2015).
RN   [2]
RP   FUNCTION.
RX   PubMed=33004788; DOI=10.1038/s41467-020-18713-0;
RA   Zheng L., Wang H., Fan A., Li S.M.;
RT   "Oxepinamide F biosynthesis involves enzymatic D-aminoacyl epimerization,
RT   3H-oxepin formation, and hydroxylation induced double bond migration.";
RL   Nat. Commun. 11:4914-4914(2020).
CC   -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of oxepinamides, derivatives of anthranilyl-containing
CC       tripeptides that share an oxepin ring and a fused pyrimidinone moiety
CC       (PubMed:33004788). The nonribosomal peptide synthetase (NRPS) opaA
CC       assembles the quinazolinone core with D-Phe incorporation
CC       (PubMed:33004788). The first adenylation domain (A1) of opaA loads and
CC       activates anthranilic acid whereas the second A domain (A2) is for
CC       activating of L-Phe, which is then converted to D-form by the E domain
CC       (PubMed:33004788). The third A domain (A3) is responsible for L-Ile
CC       activation and the terminal condensation domain C3 for cyclization and
CC       releasing the NRPS product protuboxepin K (PubMed:33004788). The
CC       cytochrome P450 monooxygenase opaB then catalyzes alone the oxepin ring
CC       formation to convert protuboxepin K into protuboxepin A
CC       (PubMed:33004788). The flavoenzyme opaC installs subsequently one
CC       hydroxyl group at the oxepin ring, accompanied by double bond
CC       migration, to form 15-epi-oxepinamide E (PubMed:33004788). The
CC       epimerase opaE changes the D-Phe residue back to L-form, leading to
CC       oxepinamide E, which is further methylated at the hydroxyl group at C-
CC       12 by the O-methyltransferase OpaF to yield oxepinamide F
CC       (PubMed:33004788). {ECO:0000269|PubMed:33004788}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:33004788}.
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; JOMC01000153; KIA75453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1E5J2; -.
DR   SMR; A0A0C1E5J2; -.
DR   EnsemblFungi; KIA75453; KIA75453; HK57_00060.
DR   Proteomes; UP000053475; Unassembled WGS sequence.
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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..420
FT                   /note="O-methyltransferase opaF"
FT                   /id="PRO_0000452998"
FT   ACT_SITE        328
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         262..263
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         308..309
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
SQ   SEQUENCE   420 AA;  46354 MW;  34652FBF341B9017 CRC64;
     MARGAAELTQ TRKVMIKEQL ANLTALIDLR IADTPCNGLD DDMPMQPAID NTITHELAKE
     TYALLHAIKG PSLSVFNFGE QVMHVSAVRA LFGLGVFSAL PQDRQAMTAT ALAEKLGCDE
     ELLVRLMRMC TIWGPFKEVG TETYSHTQFS LAYLDPQVTN QFQAFVDEFL PACLQLHKFL
     EINNGKPPVD ATNCPYTLAH QTSGKDMWEH LAQFPKRSKV VNSAMYAISS AHPWPVALYP
     FREALLQLPP TSSNAPLVID IGGGQGQAIS VIRKMCGGIN GRFILEDRPE VLAGIPHTLR
     GIEKIECDLF KPQPVKGAAI YFLRHVLHDW AEDACVRILQ NIASAITDKS TQRVVISEMV
     LPEKGVTAEC ATQDLVTLST TGAERSRKQW ERLIPAAGFR VENIYSSEAS CEAAIECYLE