ID   DMAW_BALOB              Reviewed;         465 AA.
AC   Q6X1E1;
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   Balansia obtecta.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Balansia.
OX   NCBI_TaxID=40611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Mycelium;
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; AY262013; AAP92451.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6X1E1; -.
DR   SMR; Q6X1E1; -.
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..465
FT                   /note="Tryptophan dimethylallyltransferase"
FT                   /id="PRO_0000181362"
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         249
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         262
FT                   /ligand="substrate"
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         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         418
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ   SEQUENCE   465 AA;  53932 MW;  5549517F27EED760 CRC64;
     MATENGPDKS VYETLSLIFN FPDDTQRLWW HSTAPMLAEM LQTCEYSVHN QYQQLGIFKK
     HIIPYLGVYP TKSKERWLSI LTRYGIPFEL SLNCSDSVVR YTYEPINEAT GTEKDPYNTL
     AILDSAQELI RIQAGIDLEW FTYFKDELTV NMTESEYLRS NGLVNCQIKT QNKLALDLKG
     DQFTLKVYMY PELKSVATGK SLHELIFGSV RRLSLKYNSI RAPLDMLDDY VTSRNMGANG
     EEHLPLEPRL LSCDLMDPHK SRVKIYLHER KVSLSAMEDL WTLGGRRTDS TTMDGLNMVR
     ELWDLLEIPT CLQKYPAPFL ELGQIPREQL PSMANYTLHH GDPMPEPQVY FTVFGMNDSK
     VISALTEFFK RRVWNGMARK YRAFLQNSYP NDDHESLNYL HTYISFSYRK NKPYLSVYLH
     TFESGSWPIF PDSSTAFKTY RRCDLSCKDN GLDDKLLSPV CQLRV