ID   DMAW1_EPICN             Reviewed;         448 AA.
AC   Q6X2E2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Tryptophan dimethylallyltransferase 1;
DE            EC=2.5.1.34;
DE   AltName: Full=4-dimethylallyltryptophan synthase 1;
DE   AltName: Full=All-trans-hexaprenyl-diphosphate synthase 1;
DE   AltName: Full=L-tryptophan dimethylallyl transferase 1;
DE            Short=DMATS 1;
GN   Name=dmaW1;
OS   Epichloe coenophiala (Tall fescue endophyte fungus) (Neotyphodium
OS   coenophialum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX   NCBI_TaxID=5047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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       (By similarity). {ECO:0000250}.
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; AY259838; AAP81207.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6X2E2; -.
DR   SMR; Q6X2E2; -.
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..448
FT                   /note="Tryptophan dimethylallyltransferase 1"
FT                   /id="PRO_0000181360"
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   448 AA;  52010 MW;  205474D3B7EFA10C CRC64;
     MVMAKTLHQE VYHTLSETFD FANNDQRLWW HSTAPMFEKM LQTANYSIDA QYRHLGIYKS
     HVIPFLGVYP TRSGERWLSI LTRYGTPFEL SLNCSDSVVR YTYEPINAAT GSHLDPFNTF
     AIWEALKKHI ESQPGIDLEW FSYFKQELTL DANESTYLHS QNLVKEQIKT QNKLALDLKG
     DKFVLKTYIY PELKSVATGK SVQELVFGSV RKLAQKHKSI RPAFEMLEDY VQSRNKFSTT
     DDSHNTLLSS RLLSCDLISP TKSRVKIYLL ERMVSLPAME DLWTLGGRRE DQSTIEGLEM
     IRELWGLLNM SPGLRAYPEP YLPLGAIPNE QLPSMANYTL HHNDPIPEPQ VYFTVFGMND
     MEVTNALTTF FMRHEWSDMA SKYKACLRES FPHHDYEALN YIHSYISFSY RKNKPYLSVY
     LHSFETGKWP VFPEGLIAFD ACRRDLTC