ID   FGAMT_ASPFM             Reviewed;         339 AA.
AC   B6D5I7;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=4-dimethylallyltryptophan N-methyltransferase {ECO:0000303|PubMed:18678866};
DE            EC=2.1.1.261 {ECO:0000269|PubMed:18678866};
DE   AltName: Full=4-dimethylallyltryptophan methyltransferase {ECO:0000303|PubMed:18678866};
GN   Name=fgaMT {ECO:0000303|PubMed:18678866};
OS   Neosartorya fumigata (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=746128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=NIH 5233 / ATCC 13073;
RX   PubMed=18678866; DOI=10.1074/jbc.m804979200;
RA   Rigbers O., Li S.M.;
RT   "Ergot alkaloid biosynthesis in Aspergillus fumigatus. Overproduction and
RT   biochemical characterization of a 4-dimethylallyltryptophan N-
RT   methyltransferase.";
RL   J. Biol. Chem. 283:26859-26868(2008).
CC   -!- FUNCTION: Methyltransferase that mediates the second step of
CC       biosynthesis of ergot alkaloid biosynthesis. Catalyzes the N-
CC       methylation of 4-dimethylallyl-L-tryptophan in the presence of S-
CC       adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-
CC       abrine. Ergot alkaloids, which are produced by endophyte fungi, can
CC       enhance plant host fitness, but also cause livestock toxicosis to host
CC       plants. {ECO:0000269|PubMed:18678866}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(3-methylbut-2-enyl)-L-tryptophan + S-adenosyl-L-methionine
CC         = 4-(3-methylbut-2-enyl)-L-abrine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:34435, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58209, ChEBI:CHEBI:59789, ChEBI:CHEBI:67248;
CC         EC=2.1.1.261; Evidence={ECO:0000269|PubMed:18678866};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.12 mM for 4-dimethylallyl-L-tryptophan
CC         {ECO:0000269|PubMed:18678866};
CC         KM=2.4 mM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18678866};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000269|PubMed:18678866}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18678866}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; EU827256; ACI43096.1; -; mRNA.
DR   AlphaFoldDB; B6D5I7; -.
DR   SMR; B6D5I7; -.
DR   KEGG; ag:ACI43096; -.
DR   BioCyc; MetaCyc:MON-15600; -.
DR   BRENDA; 2.1.1.261; 508.
DR   SABIO-RK; B6D5I7; -.
DR   UniPathway; UPA00327; -.
DR   GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0035837; P:ergot alkaloid biosynthetic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..339
FT                   /note="4-dimethylallyltryptophan N-methyltransferase"
FT                   /id="PRO_0000421751"
SQ   SEQUENCE   339 AA;  38034 MW;  B8A49A3433DAD6F6 CRC64;
     MTISAPPIID IRQAGLESSI PDQVVEGLTK EVKTLPALLF YSTKGIQHWN RHSHAADFYP
     RHEELCILKA EASKMAASIA QDSLVIDMGS ASMDKVILLL EALEEQKKSI TYCALDLSYS
     ELASNFQAIP VDRFHYVRFA ALHGTFDDGL HWLQNAPDIR NRPRCILLFG LTIGNFSRDN
     AASFLRNIAQ SALSTSPTQS SIIVSLDSCK LPTKILRAYT ADGVVPFALA SLSYANSLFH
     PKGDRKIFNE EDWYFHSEWN HALGRHEASL ITQSKDIQLG APLETVIVRR DEKIRFGCSY
     KYDKAERDQL FHSAGLEDAA VWTAPDCDVA FYQLRLRLN