EASF_EPIFI
ID EASF_EPIFI Reviewed; 344 AA.
AC A2TBU2;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 29.
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:17308187};
GN Name=easF {ECO:0000303|PubMed:17308187};
OS Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX NCBI_TaxID=73839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=Lp19;
RX PubMed=17308187; DOI=10.1128/aem.00257-07;
RA Fleetwood D.J., Scott B., Lane G.A., Tanaka A., Johnson R.D.;
RT "A complex ergovaline gene cluster in epichloe endophytes of grasses.";
RL Appl. Environ. Microbiol. 73:2571-2579(2007).
RN [2]
RP FUNCTION.
RX PubMed=11592979; DOI=10.1073/pnas.221198698;
RA Panaccione D.G., Johnson R.D., Wang J., Young C.A., Damrongkool P.,
RA Scott B., Schardl C.L.;
RT "Elimination of ergovaline from a grass-Neotyphodium endophyte symbiosis by
RT genetic modification of the endophyte.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12820-12825(2001).
CC -!- FUNCTION: 4-dimethylallyltryptophan N-methyltransferase; part of the
CC gene cluster that mediates the biosynthesis of fungal ergot alkaloid
CC ergovaline, the predominant ergopeptine product in E.festucae var.
CC lolii (PubMed:17308187). DmaW catalyzes the first step of ergot
CC alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP)
CC and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity).
CC The second step is catalyzed by the methyltransferase easF that
CC methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-
CC L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine
CC (By 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 The presence of easA is not required to complete this reaction (By
CC similarity). Further conversion of agroclavine to paspalic acid is a
CC two-step process involving oxidation of agroclavine to elymoclavine and
CC of elymoclavine to paspalic acid, the second step being performed by
CC the elymoclavine oxidase cloA (By similarity). Paspalic acid is then
CC further converted to D-lysergic acid (By similarity). Ergovaline is
CC assembled from D-lysergic acid and three different amino acids by the
CC D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a
CC trimodular (lpsA) nonribosomal peptide synthetase subunit
CC (PubMed:17308187, PubMed:11592979). {ECO:0000250|UniProtKB:Q50EL0,
CC ECO:0000269|PubMed:11592979, ECO:0000269|PubMed:17308187}.
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:17308187}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B6D5I7}.
CC -!- INDUCTION: Strongly expressed in planta but not expressed in axenic
CC culture (PubMed:17308187). {ECO:0000269|PubMed:17308187}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; EF125025; ABM91451.1; -; Genomic_DNA.
DR AlphaFoldDB; A2TBU2; -.
DR SMR; A2TBU2; -.
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 2: Evidence at transcript level;
KW Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..344
FT /note="4-dimethylallyltryptophan N-methyltransferase easF"
FT /id="PRO_0000439142"
SQ SEQUENCE 344 AA; 38608 MW; 9EA06B874CB927E5 CRC64;
MSKPNVLDIR LATFEDSIVD LVINGLRKQP KTLPALLFYA NEGLKHWNHH SHQPEFYPRH
QEVQILKKKA QEMAASIPMN SVVVDLGSAS LDKVIHLLEA LEVQKKNISY YALDVSASQL
ESTLAAIPTQ NFRHVRFAGL HGTFDDGLHW LKEAPEARDV PHTVLLFGLT IGNFSRPNAA
AFLSNIGQHA FQGKSGDQCS ILMSLDSCKV PTQVLRAYTC EGVVPFALQS LTYANGLFSE
KNKTQASGDV QHKVFNLDEW YYLSEWNFVL GRHEASLIPR SKDIKLLPPL DGILVSKDEK
VRFGCSYKYD QEERMELFAA AGVKNEVTWS DEGCDVAFYQ LKLS
