DMAW_TRIVH
ID DMAW_TRIVH Reviewed; 375 AA.
AC D4D449;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Tryptophan dimethylallyltransferase {ECO:0000305};
DE EC=2.5.1.34 {ECO:0000250|UniProtKB:Q50EL0};
DE AltName: Full=4-dimethylallyltryptophan synthase {ECO:0000303|PubMed:22403186};
DE Short=DMATS {ECO:0000303|PubMed:22403186};
DE AltName: Full=All-trans-hexaprenyl-diphosphate synthase {ECO:0000305};
DE AltName: Full=L-tryptophan dimethylallyl transferase {ECO:0000305};
GN Name=dmaW {ECO:0000303|PubMed:22403186}; ORFNames=TRV_01863;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP FUNCTION.
RX PubMed=22403186; DOI=10.1099/mic.0.056796-0;
RA Wallwey C., Heddergott C., Xie X., Brakhage A.A., Li S.M.;
RT "Genome mining reveals the presence of a conserved gene cluster for the
RT biosynthesis of ergot alkaloid precursors in the fungal family
RT Arthrodermataceae.";
RL Microbiology 158:1634-1644(2012).
CC -!- FUNCTION: Tryptophan dimethylallyltransferase; part of the gene cluster
CC that mediates the biosynthesis of fungal ergot alkaloid
CC (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid
CC biosynthesis by condensing dimethylallyl diphosphate (DMAP) and
CC tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). The
CC second step is catalyzed by the methyltransferase easF that methylates
CC 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-
CC methionine, resulting in the formation of 4-dimethylallyl-L-abrine
CC (PubMed:22403186). The catalase easC and the FAD-dependent
CC oxidoreductase easE then transform 4-dimethylallyl-L-abrine to
CC chanoclavine-I which is further oxidized by easD in the presence of
CC NAD(+), resulting in the formation of chanoclavine-I aldehyde
CC (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of
CC ergoamides and ergopeptines in Clavicipitaceae, and clavine-type
CC alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186).
CC However, the metabolites downstream of chanoclavine-I aldehyde in
CC Arthrodermataceae have not been identified yet (PubMed:22403186).
CC {ECO:0000269|PubMed:22403186}.
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 Evidence={ECO:0000250|UniProtKB:Q50EL0};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000305|PubMed:22403186}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q50EL0}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; ACYE01000098; EFE43383.1; -; Genomic_DNA.
DR RefSeq; XP_003024001.1; XM_003023955.1.
DR AlphaFoldDB; D4D449; -.
DR SMR; D4D449; -.
DR EnsemblFungi; EFE43383; EFE43383; TRV_01863.
DR GeneID; 9582694; -.
DR KEGG; tve:TRV_01863; -.
DR HOGENOM; CLU_037431_0_0_1; -.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000008383; 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:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 3: Inferred from homology;
KW Alkaloid metabolism; Transferase.
FT CHAIN 1..375
FT /note="Tryptophan dimethylallyltransferase"
FT /id="PRO_0000439103"
FT BINDING 83..84
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 92
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 193
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 246
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 375 AA; 42705 MW; 810A5E57B4898D89 CRC64;
MGSIEIPNCS GSIVYKTISD FIDFPDHEQK LWWHSTAPMF AEMLRVAGYD LHSQYKILGI
FLNHVIPFLG VYPTRINNRW LSILTRYGTP FELSLNCSQS LVRYTYEPIN SATGTVKDPF
NTHSIWDALD RLMPLQKGID LEFFKHLKQD LTVDDQDSAY LLENNLVGGQ IRTQNKLALD
LKGGNFVLKT YIYPALKALA TGKSIKTLMF DSVYRLCRQN PSLEAPLRAL EEYVDSKGPN
STASPRLLSC DLIDPSKSRV KIYILELNVT LEAMEDLWTM GGRLNDASTL AGLEMLRELW
DLIKLPPGMR EYPEPFLQLG TIPDEQLPLM ANYTLHHDQA MPEPQVYFTT FGLNDGRVAD
GLVTFFERRG WNHMA
