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Tryptophan dimethylallyltransferase 2 (EC 2.5.1.34) (4-dimethylallyltryptophan synthase 2) (All-trans-hexaprenyl-diphosphate synthase 2) (L-tryptophan dimethylallyl transferase 2) (DMATS 2)

 DMAW2_CLAP2             Reviewed;         448 AA.
Q9C141; M1VVX0;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 56.
RecName: Full=Tryptophan dimethylallyltransferase 2;
EC=2.5.1.34;
AltName: Full=4-dimethylallyltryptophan synthase 2;
AltName: Full=All-trans-hexaprenyl-diphosphate synthase 2;
AltName: Full=L-tryptophan dimethylallyl transferase 2;
Short=DMATS 2;
Name=dmaW2; Synonyms=cpd2; ORFNames=CPUR_04105;
Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
Claviceps.
NCBI_TaxID=1111077;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=T5;
Arntz C., Tudzynski P.;
"Molecular analysis of dimethyl-allyl-tryptophan-synthase-genes.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=20.1;
PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K.,
Calie P.J., Fleetwood D.J., Haws D.C., Moore N., Oeser B.,
Panaccione D.G., Schweri K.K., Voisey C.R., Farman M.L.,
Jaromczyk J.W., Roe B.A., O'Sullivan D.M., Scott B., Tudzynski P.,
An Z., Arnaoudova E.G., Bullock C.T., Charlton N.D., Chen L., Cox M.,
Dinkins R.D., Florea S., Glenn A.E., Gordon A., Gueldener U.,
Harris D.R., Hollin W., Jaromczyk J., Johnson R.D., Khan A.K.,
Leistner E., Leuchtmann A., Li C., Liu J., Liu J., Liu M., Mace W.,
Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K., Steiner U.,
Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
Yoshida R., Zeng Z.;
"Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of
the Clavicipitaceae reveals dynamics of alkaloid loci.";
PLoS Genet. 9:E1003323-E1003323(2013).
-!- FUNCTION: Catalyzes the first step of ergot alkaloid biosynthesis.
Ergot alkaloids, which are produced by endophyte fungi, can
enhance plant host fitness, but also cause livestock toxicosis to
host plants (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + L-tryptophan =
diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan.
-!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CCE30257.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AJ312753; CAC37396.1; -; Genomic_DNA.
EMBL; CAGA01000020; CCE30257.1; ALT_SEQ; Genomic_DNA.
ProteinModelPortal; Q9C141; -.
SMR; Q9C141; -.
EnsemblFungi; CCE30257; CCE30257; CPUR_04105.
OrthoDB; EOG092C1W0C; -.
UniPathway; UPA00327; -.
Proteomes; UP000016801; Unassembled WGS sequence.
GO; GO:0050364; F:tryptophan dimethylallyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0035837; P:ergot alkaloid biosynthetic process; IEA:InterPro.
CDD; cd13929; PT-DMATS_CymD; 1.
InterPro; IPR017795; Aro_prenylTrfase_DMATS.
InterPro; IPR012148; DMATS-type_fun.
InterPro; IPR017796; Trp_dimethylallylTrfase.
Pfam; PF11991; Trp_DMAT; 1.
PIRSF; PIRSF000509; Trp_DMAT; 1.
TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
TIGRFAMs; TIGR03430; trp_dimet_allyl; 1.
3: Inferred from homology;
Alkaloid metabolism; Complete proteome; Reference proteome;
Transferase.
CHAIN 1 448 Tryptophan dimethylallyltransferase 2.
/FTId=PRO_0000181365.
REGION 80 81 L-tryptophan binding.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 89 89 L-tryptophan.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 100 100 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 186 186 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 188 188 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 190 190 L-tryptophan.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 249 249 L-tryptophan.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 262 262 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 264 264 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 266 266 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 348 348 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 350 350 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 414 414 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
BINDING 418 418 Substrate.
{ECO:0000250|UniProtKB:Q50EL0}.
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


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