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Q12594 (DMAW_CLAFS) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tryptophan dimethylallyltransferase

EC=2.5.1.34
Alternative name(s):
4-dimethylallyltryptophan synthase
All-trans-hexaprenyl-diphosphate synthase
L-tryptophan dimethylallyl transferase
Short name=DMATS
Gene names
Name:dmaW
OrganismClaviceps fusiformis (Ergot fungus)
Taxonomic identifier40602 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesClavicipitaceaeClaviceps

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

Dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan. Ref.1 Ref.2

Pathway

Alkaloid biosynthesis; ergot alkaloid biosynthesis.

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the tryptophan dimethylallyltransferase family.

Ontologies

Keywords
   Biological processAlkaloid metabolism
   Molecular functionTransferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processalkaloid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontryptophan dimethylallyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Tryptophan dimethylallyltransferase
PRO_0000181363

Sequences

Sequence LengthMass (Da)Tools
Q12594 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A913F8E60EBBEB63

FASTA45551,858
        10         20         30         40         50         60 
MMTKAPATAV YDTLSLLFDF PNQEQRLWWH SIAPMFAAML DTAGHNVHDQ YRHLGIFKKH 

        70         80         90        100        110        120 
IIPFLGVYPA QGKHTWPSVL TRYGIPFELS LNCLDSVVRY TFEPTTEHTG TGDDSYNAFA 

       130        140        150        160        170        180 
ILECIQKLVR IQPGIDMEWF SYFRNELVLN ATESARLGRN DSVNQQPIRT QNKLALDLKG 

       190        200        210        220        230        240 
DRFALKVYLY PHLKSIATGV SSHDLIFNSV RKLSQKHTSI QPSFNVLCDY VASRNDPDSN 

       250        260        270        280        290        300 
AAEAEAGVPA SALRARLLSC DLVDPSKSRI KIYLLEQTVS LTAMEDLWTL GGRRTDSSTL 

       310        320        330        340        350        360 
NGLDMMRELW HLLQIPSGFM KYPESDLKLG EVPDEQLPSM VHYALHPDQP MPEPQVYFTV 

       370        380        390        400        410        420 
FGMSDAGITN ALATFFSRHG WYEMAKKYRV FLEGSFPNHD FESLNYLHTY VSFSYRKNKP 

       430        440        450 
YLSVYLHSFE TGQWPAFSDD PTAFNAFKRC DLSLT 

« Hide

References

[1]"The Claviceps purpurea gene encoding dimethylallyltryptophan synthase, the committed step for ergot alkaloid biosynthesis."
Tsai H.-F., Wang H., Gebler J.C., Poulter C.D., Schardl C.L.
Biochem. Biophys. Res. Commun. 216:119-125(1995) [PubMed: 7488077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 340-349; 351-360 AND 384-407, ENZYME ACTIVITY.
[2]"Purification and characterization of dimethylallyl tryptophan synthase from Claviceps purpurea."
Gebler J.C., Poulter C.D.
Arch. Biochem. Biophys. 296:308-313(1992) [PubMed: 1605639] [Abstract]
Cited for: ENZYME ACTIVITY, HOMODIMERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L39640 Genomic DNA. Translation: AAC18893.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017795. Aromatic_prenylTrfase_DMATS.
IPR012148. Trp_dimethylallyltransferase.
IPR017796. Trp_dimethylallylTrfase_sub.
[Graphical view]
PfamPF11991. Trp_DMAT. 1 hit.
[Graphical view]
PIRSFPIRSF000509. Trp_DMAT. 1 hit.
TIGRFAMsTIGR03429. Arom_pren_DMATS. 1 hit.
TIGR03430. Trp_dimet_allyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDMAW_CLAFS
AccessionPrimary (citable) accession number: Q12594
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1996
Last modified: October 19, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families