DMAW2_EPICN
ID DMAW2_EPICN Reviewed; 450 AA.
AC Q6X2E1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Tryptophan dimethylallyltransferase 2;
DE EC=2.5.1.34;
DE AltName: Full=4-dimethylallyltryptophan synthase 2;
DE AltName: Full=All-trans-hexaprenyl-diphosphate synthase 2;
DE AltName: Full=L-tryptophan dimethylallyl transferase 2;
DE Short=DMATS 2;
GN Name=dmaW2;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY259839; AAP81208.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6X2E1; -.
DR SMR; Q6X2E1; -.
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 2"
FT /id="PRO_0000181361"
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
