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Protein

Tryptophan dimethylallyltransferase

Gene

dmaW

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460, PubMed:23435153). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD+, resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).By similarity8 Publications

Catalytic activityi

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

Kineticsi

  1. KM=4 µM for dimethylallyl diphosphate1 Publication
  2. KM=8 µM for L-tryptophan1 Publication
  1. Vmax=0.198 µmol/min/mg enzyme1 Publication

Pathwayi: ergot alkaloid biosynthesis

This protein is involved in the pathway ergot alkaloid biosynthesis, which is part of Alkaloid biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in the pathway ergot alkaloid biosynthesis and in Alkaloid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei89L-tryptophan1 Publication1
Binding sitei100Substrate1 Publication1
Binding sitei187Substrate1 Publication1
Binding sitei189Substrate1 Publication1
Binding sitei191L-tryptophan1 Publication1
Binding sitei244L-tryptophan1 Publication1
Binding sitei257Substrate1 Publication1
Binding sitei259Substrate1 Publication1
Binding sitei261Substrate1 Publication1
Binding sitei343Substrate1 Publication1
Binding sitei345Substrate1 Publication1
Binding sitei409Substrate1 Publication1
Binding sitei413Substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Alkaloid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15369.
BRENDAi2.5.1.34. 508.
SABIO-RKQ50EL0.
UniPathwayiUPA00327.

Protein family/group databases

MEROPSiM77.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan dimethylallyltransferaseCurated (EC:2.5.1.341 Publication)
Alternative name(s):
4-dimethylallyltryptophan synthase1 Publication
All-trans-hexaprenyl-diphosphate synthaseCurated
L-tryptophan dimethylallyl transferaseCurated
Short name:
DMATSCurated
Gene namesi
Name:dmaW1 Publication
Synonyms:fgaPT21 Publication
ORF Names:AFUA_2G18040
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiFungiDB:Afu2g18040.

Pathology & Biotechi

Biotechnological usei

Ergot alkaloids are known for their toxic effects on humans who consume contaminated grains or livestock that graze on grasses harboring ergot alkaloid-producing fungi (PubMed:19523108). Due to their strong affinity for monoamine neurotransmitter receptors they may also have clinical uses such as treatment of migraines, Parkinson's disease and cerebrovascular insufficiency (PubMed:19523108).1 Publication

Disruption phenotypei

Impairs the production of ergot alkaloids including festuclavine, fumigaclavine A, fumigaclavine B and fumigaclavine C (PubMed:15933009).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi89E → A: Abolishes tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi100R → D or Q: Nearly abolishes tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi174K → E: Nearly abolishess tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi174K → Q: Impairs tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi187K → E: Nearly abolishes tryptophan dimethylallyltransferase activity. 1 Publication1
Mutagenesisi259K → E: Nearly abolishes tryptophan dimethylallyltransferase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002286871 – 459Tryptophan dimethylallyltransferaseAdd BLAST459

Proteomic databases

PRIDEiQ50EL0.

Expressioni

Inductioni

The expression of the ergot alkaloid synthesis cluster which leads to the synthesis of fumigaclavines is positively regulated by the brlA and stuA transcription factors (PubMed:19028996).1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Helixi10 – 18Combined sources9
Helixi24 – 43Combined sources20
Helixi48 – 61Combined sources14
Helixi63 – 65Combined sources3
Beta strandi72 – 74Combined sources3
Beta strandi87 – 93Combined sources7
Turni94 – 97Combined sources4
Beta strandi98 – 103Combined sources6
Helixi122 – 129Combined sources8
Helixi130 – 132Combined sources3
Helixi139 – 148Combined sources10
Helixi152 – 160Combined sources9
Helixi162 – 164Combined sources3
Turni165 – 167Combined sources3
Beta strandi173 – 180Combined sources8
Beta strandi183 – 190Combined sources8
Helixi193 – 199Combined sources7
Helixi203 – 217Combined sources15
Helixi219 – 221Combined sources3
Helixi222 – 234Combined sources13
Beta strandi240 – 251Combined sources12
Turni253 – 255Combined sources3
Beta strandi258 – 264Combined sources7
Beta strandi266 – 268Combined sources3
Helixi269 – 276Combined sources8
Turni277 – 281Combined sources5
Helixi285 – 301Combined sources17
Beta strandi327 – 333Combined sources7
Beta strandi341 – 346Combined sources6
Helixi353 – 366Combined sources14
Helixi370 – 383Combined sources14
Helixi389 – 391Combined sources3
Beta strandi394 – 404Combined sources11
Beta strandi407 – 414Combined sources8
Helixi420 – 424Combined sources5
Helixi448 – 450Combined sources3
Beta strandi451 – 454Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3I4XX-ray2.10A/B1-459[»]
3I4ZX-ray1.76A/B1-459[»]
ProteinModelPortaliQ50EL0.
SMRiQ50EL0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ50EL0.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni80 – 81L-tryptophan binding1 Publication2

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000200278.
InParanoidiQ50EL0.
KOiK14130.
OrthoDBiEOG092C1XRO.

Family and domain databases

CDDicd13929. PT-DMATS_CymD. 1 hit.
InterProiIPR033964. Aro_prenylTrfase.
IPR017795. Aro_prenylTrfase_DMATS.
IPR012148. DMATS-type_fun.
IPR017796. Trp_dimethylallylTrfase.
[Graphical view]
PANTHERiPTHR40627. PTHR40627. 1 hit.
PfamiPF11991. Trp_DMAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000509. Trp_DMAT. 1 hit.
TIGRFAMsiTIGR03429. arom_pren_DMATS. 1 hit.
TIGR03430. trp_dimet_allyl. 1 hit.

Sequencei

Sequence statusi: Complete.

Q50EL0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAANASSAE AYRVLSRAFR FDNEDQKLWW HSTAPMFAKM LETANYTTPC
60 70 80 90 100
QYQYLITYKE CVIPSLGCYP TNSAPRWLSI LTRYGTPFEL SLNCSNSIVR
110 120 130 140 150
YTFEPINQHT GTDKDPFNTH AIWESLQHLL PLEKSIDLEW FRHFKHDLTL
160 170 180 190 200
NSEESAFLAH NDRLVGGTIR TQNKLALDLK DGRFALKTYI YPALKAVVTG
210 220 230 240 250
KTIHELVFGS VRRLAVREPR ILPPLNMLEE YIRSRGSKST ASPRLVSCDL
260 270 280 290 300
TSPAKSRIKI YLLEQMVSLE AMEDLWTLGG RRRDASTLEG LSLVRELWDL
310 320 330 340 350
IQLSPGLKSY PAPYLPLGVI PDERLPLMAN FTLHQNDPVP EPQVYFTTFG
360 370 380 390 400
MNDMAVADAL TTFFERRGWS EMARTYETTL KSYYPHADHD KLNYLHAYIS
410 420 430 440 450
FSYRDRTPYL SVYLQSFETG DWAVANLSES KVKCQDAACQ PTSLPPDLSK

TGVYYSGLH
Length:459
Mass (Da):52,463
Last modified:March 21, 2006 - v2
Checksum:iED7AAB193E9A46C8
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti443S → A in strain: B5233 / ATCC 13073. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY775787 mRNA. Translation: AAX08549.1.
AAHF01000001 Genomic DNA. Translation: EAL94103.2. Sequence problems.
RefSeqiXP_756141.2. XM_751048.2.

Genome annotation databases

GeneIDi3512716.
KEGGiafm:AFUA_2G18040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY775787 mRNA. Translation: AAX08549.1.
AAHF01000001 Genomic DNA. Translation: EAL94103.2. Sequence problems.
RefSeqiXP_756141.2. XM_751048.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3I4XX-ray2.10A/B1-459[»]
3I4ZX-ray1.76A/B1-459[»]
ProteinModelPortaliQ50EL0.
SMRiQ50EL0.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM77.004.

Proteomic databases

PRIDEiQ50EL0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3512716.
KEGGiafm:AFUA_2G18040.

Organism-specific databases

EuPathDBiFungiDB:Afu2g18040.

Phylogenomic databases

HOGENOMiHOG000200278.
InParanoidiQ50EL0.
KOiK14130.
OrthoDBiEOG092C1XRO.

Enzyme and pathway databases

UniPathwayiUPA00327.
BioCyciMetaCyc:MONOMER-15369.
BRENDAi2.5.1.34. 508.
SABIO-RKQ50EL0.

Miscellaneous databases

EvolutionaryTraceiQ50EL0.

Family and domain databases

CDDicd13929. PT-DMATS_CymD. 1 hit.
InterProiIPR033964. Aro_prenylTrfase.
IPR017795. Aro_prenylTrfase_DMATS.
IPR012148. DMATS-type_fun.
IPR017796. Trp_dimethylallylTrfase.
[Graphical view]
PANTHERiPTHR40627. PTHR40627. 1 hit.
PfamiPF11991. Trp_DMAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000509. Trp_DMAT. 1 hit.
TIGRFAMsiTIGR03429. arom_pren_DMATS. 1 hit.
TIGR03430. trp_dimet_allyl. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDMAW_ASPFU
AccessioniPrimary (citable) accession number: Q50EL0
Secondary accession number(s): Q4WZ62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: November 30, 2016
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.