ID   BENX_ASPTE              Reviewed;         361 AA.
AC   P9WEU7;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=N-methyltransferase benX {ECO:0000303|PubMed:28604695};
DE            EC=2.1.1.- {ECO:0000305|PubMed:28604695};
DE   AltName: Full=Benzomalvin biosynthesis cluster protein X {ECO:0000303|PubMed:28604695};
GN   Name=benX {ECO:0000303|PubMed:28604695};
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=ATCC 20542 / MF4845;
RX   PubMed=28604695; DOI=10.1038/nchembio.2408;
RA   Clevenger K.D., Bok J.W., Ye R., Miley G.P., Verdan M.H., Velk T., Chen C.,
RA   Yang K., Robey M.T., Gao P., Lamprecht M., Thomas P.M., Islam M.N.,
RA   Palmer J.M., Wu C.C., Keller N.P., Kelleher N.L.;
RT   "A scalable platform to identify fungal secondary metabolites and their
RT   gene clusters.";
RL   Nat. Chem. Biol. 13:895-901(2017).
CC   -!- FUNCTION: N-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of benzomalvin A and D (PubMed:28604695). The pathway
CC       begins with the loading of amino acid precursors onto the A domains of
CC       the non ribosomal peptide synthetases benY and benZ (PubMed:28604695).
CC       BenY and the A1 domain of benZ are loaded with anthranilate (Anth),
CC       while the A2 domain of benZ is loaded with phenylalanine (Phe)
CC       (PubMed:28604695). N-methylation of Phe by the methyltransferase benX
CC       may happen before loading of Phe onto benZ, after loading of Phe, or
CC       after dipeptide formation (PubMed:28604695). Condensation of Anth with
CC       the secondary amine of NmPhe or Phe is catalyzed by the C1 domain of
CC       benZ, forming a dipeptide intermediate (PubMed:28604695). This is
CC       followed by in trans condensation of the Anth-NmPhe dipeptide with Anth
CC       bound to the T domain of benY by the C2 domain of benZ to form the
CC       linear tripeptide Anth-NmPhe-Anth (PubMed:28604695). Cyclization and
CC       release of the tripeptide is then catalyzed by the C-terminal C domain
CC       of benY and the resulting 11-member macrocyclic intermediate is
CC       expected to spontaneously collapse to form the benzodiazepine core
CC       (PubMed:28604695). Benzomalvin A is in conformational equilibrium with
CC       its atropisomer, benzomalvin D (PubMed:28604695).
CC       {ECO:0000269|PubMed:28604695}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:28604695}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a tenfold decrease in the amount of
CC       benzomalvins A and D, but not their complete abolishment.
CC       {ECO:0000269|PubMed:28604695}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; KX449366; AQM58289.1; -; Genomic_DNA.
DR   AlphaFoldDB; P9WEU7; -.
DR   SMR; P9WEU7; -.
DR   VEuPathDB; FungiDB:ATEG_02436; -.
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; IPR019257; MeTrfase_dom.
DR   InterPro; IPR017804; MeTrfase_EgtD-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR017805; SAM_MeTrfase_EasF-type_put.
DR   Pfam; PF10017; Methyltransf_33; 1.
DR   PIRSF; PIRSF018005; UCP018005; 1.
DR   TIGRFAMs; TIGR03439; methyl_EasF; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..361
FT                   /note="N-methyltransferase benX"
FT                   /id="PRO_0000450603"
SQ   SEQUENCE   361 AA;  40175 MW;  A00C68F8C4CC455E CRC64;
     MSAVEIPHPS GCRVYDIRQQ AQGSMNLQTA ITDGLLSTPK TLPSLLLWDA EGLRLFDEFA
     HSASYYLRDK ELTILRDRSH EIVTVVPAQS ILVELGSLQK TGRLIRALEK QQKPVRYYAV
     DVSLSGLTNS LTELRKELGD LHFVDITGLL GTYDDCVNWI SNPSGQDPMS SPTVTFLWMG
     NSISNLNHYI DSSSLLSQFR LACDASRLRC QFLIAADACQ DAQVVRTAYD AQNPTLRAFL
     LNGLSHANSV LGRAAFSPQD WSCESGFYPE QGQLEVYYVP LRDVELDVGG DRVYRVQRGE
     RVRAISSGKW GKKLMGRVAC AAGFQMNHAW GDSAGQYYFY HLYGGTQTFT SGNERVSVAH
     R