DMAW2_CLAP2
ID DMAW2_CLAP2 Reviewed; 448 AA.
AC Q9C141; M1VVX0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 69.
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; Synonyms=cpd2; ORFNames=CPUR_04105;
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T5;
RA Arntz C., Tudzynski P.;
RT "Molecular analysis of dimethyl-allyl-tryptophan-synthase-genes.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1;
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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 -!- SEQUENCE CAUTION:
CC Sequence=CCE30257.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ312753; CAC37396.1; -; Genomic_DNA.
DR EMBL; CAGA01000020; CCE30257.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q9C141; -.
DR SMR; Q9C141; -.
DR STRING; 1111077.Q9C141; -.
DR EnsemblFungi; CCE30257; CCE30257; CPUR_04105.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR HOGENOM; CLU_037431_0_0_1; -.
DR OrthoDB; 1531660at2759; -.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
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; Reference proteome; Transferase.
FT CHAIN 1..448
FT /note="Tryptophan dimethylallyltransferase 2"
FT /id="PRO_0000181365"
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 448 AA; 51521 MW; 1ED9FE8900810E59 CRC64;
MSTAKDPGNG VYEILSLIFD FPSNEQRLWW HSTAPMFAAM LDNAGYSVHD QYRHLSIFKT
HIIPFLGVYP TKGQERWLSI LTRCGLPLEL SLNCTDSVVR YAYEPINEMT GTEKDPSNTL
PIIGSVQKLA QIQAGIDLEW FSYFKDELTL DESESAILQD TELVKEQIKT QNKLALDLKE
SQFALKVYFY PHLKSIATGN STHFLIFDSV FKLSQKHDSI QPAFQALCDY VSRRNDSSEV
DQHRALHARL LSCDLIDPAK SRVKIYLQEQ TVSLPAMEDL WTLGGRRVDA STMDGLDMLR
ELWSLLKVPT GHLEYPKGYM ELGEIPNEQL PSLVNYTLHR NDPMPEPQVY FTVFGMNDAE
ISNALTIFLQ RHGFADMAKK YRVFLQDSYP YHDFESLNYL HSLVSFSYRR NKPYLSVYLH
TFETGRWPVV ADSPISFDAY RRCDLSTK
