ID   IMQF_ASPFN              Reviewed;         369 AA.
AC   B8NI23;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=N-methyltransferase imqF {ECO:0000303|PubMed:29182847};
DE            EC=2.1.1.- {ECO:0000305|PubMed:29182847};
DE   AltName: Full=Imizoquin biosynthesis cluster protein F {ECO:0000303|PubMed:29182847};
GN   Name=imqF {ECO:0000303|PubMed:29182847}; ORFNames=AFLA_064280;
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 [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).
RN   [2]
RP   INDUCTION, FUNCTION, AND PATHWAY.
RX   PubMed=29182847; DOI=10.1021/acschembio.7b00731;
RA   Khalid S., Baccile J.A., Spraker J.E., Tannous J., Imran M.,
RA   Schroeder F.C., Keller N.P.;
RT   "NRPS-derived isoquinolines and lipopetides mediate antagonism between
RT   plant pathogenic fungi and bacteria.";
RL   ACS Chem. Biol. 13:171-179(2018).
CC   -!- FUNCTION: N-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids
CC       that serve a protective role against oxidative stress that are
CC       essential for normal germination (PubMed:29182847). ImqB is a canonical
CC       three-module NRPS that assembles the tripeptide backbone of the
CC       imizoquins via condensation of Trp, Tyr, and Leu-derived precursors
CC       (PubMed:29182847). N-methylation by imqF and phenol oxidation by imqC,
CC       followed by cyclization via the FAD-dependent oxidase imqH carry out
CC       the three-step transformation of L-tyrosine into tetrahydroisoquinoline
CC       (PubMed:29182847). Importantly, this sequence requires the presence of
CC       a free amine in the tyrosine moiety, indicating that isoquinoline
CC       formation occurs prior to peptide bond formation (PubMed:29182847). The
CC       imidazolidin-4-one ring of imizoquins could form following additional
CC       oxidation of the methyl-derived bridgehead carbon by imqH
CC       (PubMed:29182847). Lastly, O-methylation by imqG and leucine
CC       hydroxylation by imqE complete biosynthesis of the imizoquins
CC       (PubMed:29182847). {ECO:0000269|PubMed:29182847}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29182847}.
CC   -!- INDUCTION: Expression is down-regulated by ralstonins, lipopeptides
CC       produced by the plant pathogenic bacteria Ralstonia solanacearum
CC       (PubMed:29182847). Expression is positively regulated by the imizoquins
CC       cluster-specific transcription regulator imqK (PubMed:29182847).
CC       {ECO:0000269|PubMed:29182847}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; EQ963479; EED49607.1; -; Genomic_DNA.
DR   RefSeq; XP_002379988.1; XM_002379947.1.
DR   AlphaFoldDB; B8NI23; -.
DR   SMR; B8NI23; -.
DR   STRING; 332952.B8NI23; -.
DR   EnsemblFungi; EED49607; EED49607; AFLA_064280.
DR   VEuPathDB; FungiDB:AFLA_064280; -.
DR   eggNOG; ENOG502SQAU; Eukaryota.
DR   HOGENOM; CLU_049766_0_2_1; -.
DR   OMA; KYLWDET; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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   2: Evidence at transcript level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..369
FT                   /note="N-methyltransferase imqF"
FT                   /id="PRO_0000444538"
SQ   SEQUENCE   369 AA;  41349 MW;  0ABC86A8CCF486E3 CRC64;
     MMTEAQGPVV SIGSATVTYD HPPIISPVSY PKARPTQILD IRKRTSRIDL YHEILAGLRA
     KDKELPSLLL WNDRGLDLFS EILNSDEYYP RRRETQLLQT HVNEFTRSIS SGERLIELGA
     GNLQKTVSVL RCLEQSRKHV EYCALDVSHA ALQASITELK AQLPFASYVT IRGLLGTYND
     CASWLKQSGA TVRTTFLWLG NSIANFEPED ATSILADFLQ TKASPSHSPQ MIIAVDGCQD
     VEQILEAYDM PNKLSQKFVF NGLSHANQIL GSEVFRPQHW TFEGKWNPVK SMHESFYVAK
     KPMSLDIGNE RFHVHAGEKI RAITSGKWPK DKVTSICQSA GIKVLKGWTD EEGSYGKRVT
     QVYSRGSSC