ID   DMAW_EPINE              Reviewed;         450 AA.
AC   Q6X2E3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Tryptophan dimethylallyltransferase;
DE            EC=2.5.1.34;
DE   AltName: Full=4-dimethylallyltryptophan synthase;
DE   AltName: Full=All-trans-hexaprenyl-diphosphate synthase;
DE   AltName: Full=L-tryptophan dimethylallyl transferase;
DE            Short=DMATS;
GN   Name=dmaW;
OS   Epichloe typhina x Neotyphodium lolii (Neotyphodium sp. (strain Lp1)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX   NCBI_TaxID=1915362;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=14732265; DOI=10.1016/j.fgb.2003.10.002;
RA   Wang J., Machado C., Panaccione D.G., Tsai H.-F., Schardl C.L.;
RT   "The determinant step in ergot alkaloid biosynthesis by an endophyte of
RT   perennial ryegrass.";
RL   Fungal Genet. Biol. 41:189-198(2004).
CC   -!- FUNCTION: Catalyzes the first step of ergot alkaloid biosynthesis.
CC       Ergot alkaloids, which are produced by endophyte fungi, can enhance
CC       plant host fitness, but also cause livestock toxicosis to host plants.
CC       {ECO:0000269|PubMed:14732265}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + L-tryptophan = 4-(3-methylbut-2-
CC         enyl)-L-tryptophan + diphosphate; Xref=Rhea:RHEA:14173,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57912,
CC         ChEBI:CHEBI:58209; EC=2.5.1.34;
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AY259837; AAP81206.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6X2E3; -.
DR   SMR; Q6X2E3; -.
DR   UniPathway; UPA00327; -.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR   GO; GO:0050364; F:tryptophan dimethylallyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035837; P:ergot alkaloid biosynthetic process; IEA:InterPro.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
DR   InterPro; IPR033964; Aro_prenylTrfase.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   InterPro; IPR012148; DMATS-type_fun.
DR   InterPro; IPR017796; Trp_dimethylallylTrfase.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   PIRSF; PIRSF000509; Trp_DMAT; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
DR   TIGRFAMs; TIGR03430; trp_dimet_allyl; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; Transferase.
FT   CHAIN           1..450
FT                   /note="Tryptophan dimethylallyltransferase"
FT                   /id="PRO_0000181366"
FT   BINDING         80..81
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         89
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         190
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         251
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         416
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         420
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ   SEQUENCE   450 AA;  52226 MW;  4BA1D1F6C1E0BEC0 CRC64;
     MVLAKTLHQE VYQTLSETFD FANNDQRLWW HSTAPMFQKI LQTANYSIYA QYQHLSIYKS
     HIIPFLGVYP TRSGERWLSI LTRYGTPFEL SLNCSDSIVR YTYEPINAAT GSHLDPFNTF
     AIWEALKKLI DSQPGIDLQW FSYFKQELTL DANESTYLHS QNLVKEQIKT QNKLALDLKG
     DKFVLKTYIY PELKSVATGK SVQELVFGSV RKLAQKHKSI RPAFEMLEDY VQSRNKVPTT
     DDSHNTPLSS RLLSCDLVSP TKSRVKIYLL ERMVSLPAME DLWTLGGRRE DQSTIEGLEM
     IRELWGLLNM SPGLRAYPEP YLPLGAIPNE QLPSMANYTL HHNDPIPEPQ VYFTVFGMND
     MEVTNALTKF FMRHEWSDMA SKYKACLRES FPHHNYEALN YIHSYISFSY RNNKPYLSVY
     LHSFETGEWP VFPEGLIAFD GCRRDLTCYK