ID   EASF_CLAFS              Reviewed;         355 AA.
AC   A8C7S0;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=4-dimethylallyltryptophan N-methyltransferase easF {ECO:0000250|UniProtKB:B6D5I7};
DE            EC=2.1.1.261 {ECO:0000250|UniProtKB:B6D5I7};
DE   AltName: Full=4-dimethylallyltryptophan methyltransferase {ECO:0000250|UniProtKB:B6D5I7};
DE   AltName: Full=Ergot alkaloid synthesis protein F {ECO:0000303|PubMed:17720822};
GN   Name=easF {ECO:0000303|PubMed:17720822};
OS   Claviceps fusiformis (Ergot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=40602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 26245 / DSM 2942 / CBS 164.59;
RX   PubMed=17720822; DOI=10.1128/aem.01040-07;
RA   Lorenz N., Wilson E.V., Machado C., Schardl C.L., Tudzynski P.;
RT   "Comparison of ergot alkaloid biosynthesis gene clusters in Claviceps
RT   species indicates loss of late pathway steps in evolution of C.
RT   fusiformis.";
RL   Appl. Environ. Microbiol. 73:7185-7191(2007).
CC   -!- FUNCTION: 4-dimethylallyltryptophan N-methyltransferase; part of the
CC       gene cluster that mediates the biosynthesis of fungal ergot alkaloid
CC       (PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid
CC       biosynthesis by condensing dimethylallyl diphosphate (DMAP) and
CC       tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). The
CC       second step is catalyzed by the methyltransferase easF that methylates
CC       4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-
CC       methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By
CC       similarity). The catalase easC and the FAD-dependent oxidoreductase
CC       easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is
CC       further oxidized by easD in the presence of NAD(+), resulting in the
CC       formation of chanoclavine-I aldehyde (By similarity). Agroclavine
CC       dehydrogenase easG then mediates the conversion of chanoclavine-I
CC       aldehyde to agroclavine via a non-enzymatic adduct reaction: the
CC       substrate is an iminium intermediate that is formed spontaneously from
CC       chanoclavine-I aldehyde in the presence of glutathione (By similarity).
CC       Further conversion of agroclavine to paspalic acid is a two-step
CC       process involving oxidation of agroclavine to elymoclavine and of
CC       elymoclavine to paspalic acid, the second step being performed by the
CC       elymoclavine oxidase cloA (PubMed:17720822). However, cloA does not
CC       encode a functional enzyme indicating that C.fusiformis terminates its
CC       ergot alkaloid pathway at elymoclavine (PubMed:17720822).
CC       {ECO:0000250|UniProtKB:Q5G5T6, ECO:0000269|PubMed:17720822}.
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:0000250|UniProtKB:B6D5I7};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:17720822}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B6D5I7}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; EU006773; ABV57824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8C7S0; -.
DR   SMR; A8C7S0; -.
DR   UniPathway; UPA00327; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
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   Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..355
FT                   /note="4-dimethylallyltryptophan N-methyltransferase easF"
FT                   /id="PRO_0000439141"
SQ   SEQUENCE   355 AA;  39955 MW;  95308EA791B8DF98 CRC64;
     MPACSVTDIR SHVVEDSLPD QVIKGLKSSP KTLPALLFYS NEGLDHWNHH VSQPDFYPRH
     QEVDILKQRG DEMARAIAPN SVILDLGSAN LEKVVHLLKA LEAQGKDVTY FALDISAPQL
     EVTLNEIPTS EFRHVRFAGL HGTFEDGLRW ISETPHICDL PHCVLLLGLT IGNFSRASAA
     TFLGNIASQA LRGASKDQSS ILMSLDSCKV PTQILRAYTS NGVEPFALQS LTFAKTLLRG
     PMLHNDSDEP LPCYLQPDDW YYHSEWNFVL GRHEASLIPR YRDVHLGSLL QDITVKKDEK
     IRFGCSYKYD DMERHQLFLD AGVEQDVAWT NEGCDVVIYE LKKRSNTEKL GIDRN