ID   EASF_ARTBC              Reviewed;         340 AA.
AC   D4AK46;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
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:22403186};
GN   Name=easF {ECO:0000303|PubMed:22403186}; ORFNames=ARB_04647;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   FUNCTION.
RX   PubMed=22403186; DOI=10.1099/mic.0.056796-0;
RA   Wallwey C., Heddergott C., Xie X., Brakhage A.A., Li S.M.;
RT   "Genome mining reveals the presence of a conserved gene cluster for the
RT   biosynthesis of ergot alkaloid precursors in the fungal family
RT   Arthrodermataceae.";
RL   Microbiology 158:1634-1644(2012).
CC   -!- FUNCTION: 4-dimethylallyltryptophan N-methyltransferase; part of the
CC       gene cluster that mediates the biosynthesis of fungal ergot alkaloid
CC       (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid
CC       biosynthesis by condensing dimethylallyl diphosphate (DMAP) and
CC       tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). 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
CC       (PubMed:22403186). The catalase easC and the FAD-dependent
CC       oxidoreductase easE then transform 4-dimethylallyl-L-abrine to
CC       chanoclavine-I which is further oxidized by easD in the presence of
CC       NAD(+), resulting in the formation of chanoclavine-I aldehyde
CC       (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of
CC       ergoamides and ergopeptines in Clavicipitaceae, and clavine-type
CC       alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186).
CC       However, the metabolites downstream of chanoclavine-I aldehyde in
CC       Arthrodermataceae have not been identified yet (PubMed:22403186).
CC       {ECO:0000269|PubMed:22403186}.
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:22403186}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B6D5I7}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; ABSU01000001; EFE37119.1; -; Genomic_DNA.
DR   RefSeq; XP_003017764.1; XM_003017718.1.
DR   AlphaFoldDB; D4AK46; -.
DR   SMR; D4AK46; -.
DR   STRING; 663331.D4AK46; -.
DR   EnsemblFungi; EFE37119; EFE37119; ARB_04647.
DR   GeneID; 9522610; -.
DR   KEGG; abe:ARB_04647; -.
DR   eggNOG; ENOG502SISP; Eukaryota.
DR   HOGENOM; CLU_049766_0_0_1; -.
DR   OMA; FGCSYKY; -.
DR   UniPathway; UPA00327; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
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; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..340
FT                   /note="4-dimethylallyltryptophan N-methyltransferase easF"
FT                   /id="PRO_0000439138"
SQ   SEQUENCE   340 AA;  38039 MW;  0507223A98628B68 CRC64;
     MGSINPPQIL DIRRSKFEES IPKQVEAGLL SSPKTLPALL FYSTEGIQHW NRHSHASDFY
     PRHEEIQILK DKATDMAASI ADGSVVVDLG SASLDKVIHL LEALEAAQKK VTYYALDLSF
     SELTSTLQAI PTDQFVHVQF SALHGTFDDG LQWLKETPVI RDQPHCLLLF GLTIGNFSRS
     NAAKFLHNIA SHALVESPSQ SSILLTLDSC KVPTKVTRAY TAEGVVPFAL ESLKYGNTLF
     QQDGGENVFD PEDWYFLSEW NYVLGRHEAS LVPRSKDIKL GRPLDKIVVG KHEKVRFGCS
     YKYDSEERKE LFGTAGLRDV KSWSKEGCDV AFYQLKCCPN