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Q50EL0 (DMAW_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:fgaPT2
ORF Names:AFUA_2G18040
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length459 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. Ref.1

Catalytic activity

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

Pathway

Alkaloid biosynthesis; ergot alkaloid biosynthesis.

Subunit structure

Homodimer. Ref.1

Sequence similarities

Belongs to the tryptophan dimethylallyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=4 µM for dimethylallyl diphosphate Ref.1

KM=8 µM for L-tryptophan

Vmax=0.198 µmol/min/mg enzyme

Sequence caution

The sequence EAL94103.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processAlkaloid metabolism
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Reference proteome
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 – 459459Tryptophan dimethylallyltransferase
PRO_0000228687

Natural variations

Natural variant4431S → A in strain: B5233 / ATCC 13073.

Secondary structure

1 ..................................................................... 459
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q50EL0 [UniParc].

Last modified March 21, 2006. Version 2.
Checksum: ED7AAB193E9A46C8

FASTA45952,463
        10         20         30         40         50         60 
MKAANASSAE AYRVLSRAFR FDNEDQKLWW HSTAPMFAKM LETANYTTPC QYQYLITYKE 

        70         80         90        100        110        120 
CVIPSLGCYP TNSAPRWLSI LTRYGTPFEL SLNCSNSIVR YTFEPINQHT GTDKDPFNTH 

       130        140        150        160        170        180 
AIWESLQHLL PLEKSIDLEW FRHFKHDLTL NSEESAFLAH NDRLVGGTIR TQNKLALDLK 

       190        200        210        220        230        240 
DGRFALKTYI YPALKAVVTG KTIHELVFGS VRRLAVREPR ILPPLNMLEE YIRSRGSKST 

       250        260        270        280        290        300 
ASPRLVSCDL TSPAKSRIKI YLLEQMVSLE AMEDLWTLGG RRRDASTLEG LSLVRELWDL 

       310        320        330        340        350        360 
IQLSPGLKSY PAPYLPLGVI PDERLPLMAN FTLHQNDPVP EPQVYFTTFG MNDMAVADAL 

       370        380        390        400        410        420 
TTFFERRGWS EMARTYETTL KSYYPHADHD KLNYLHAYIS FSYRDRTPYL SVYLQSFETG 

       430        440        450 
DWAVANLSES KVKCQDAACQ PTSLPPDLSK TGVYYSGLH

« Hide

References

« Hide 'large scale' references
[1]"Overproduction, purification and characterization of FgaPT2, a dimethylallyltryptophan synthase from Aspergillus fumigatus."
Unsoeld I.A., Li S.-M.
Microbiology 151:1499-1505(2005) [PubMed: 15870460] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: B5233 / ATCC 13073.
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY775787 mRNA. Translation: AAX08549.1.
AAHF01000001 Genomic DNA. Translation: EAL94103.2. Sequence problems.
RefSeqXP_756141.2. XM_751048.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3I4XX-ray2.10A/B1-459[»]
3I4ZX-ray1.76A/B1-459[»]
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3512716.
GenomeReviewsGene locus fgaPT2 in contig CM000170_GR.
KEGGafm:AFUA_2G18040.

Phylogenomic databases

GeneTreeEFGT00050000005069.
HOGENOMHBG325644.
OrthoDBEOG498Z83.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15369.
BRENDA2.5.1.34. 508.

Family and domain databases

InterProIPR017795. Aromatic_prenylTrfase_DMATS.
IPR012148. Trp_dimethylallyltransferase.
IPR017796. Trp_dimethylallylTrfase_sub.
[Graphical view]
KOK14130.
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_ASPFU
AccessionPrimary (citable) accession number: Q50EL0
Secondary accession number(s): Q4WZ62
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: December 14, 2011
This is version 44 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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