Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 70 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Tryptophan dimethylallyltransferase

Gene

dmaW

Organism
Claviceps fusiformis (Ergot fungus)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:7488077, PubMed:17720822, PubMed:1605639). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:7488077, PubMed:1605639). 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 (By similarity). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:17720822). However, cloA does not encode a functional enzyme indicating that C.fusiformis terminates its ergot alkaloid pathway at elymoclavine (PubMed:17720822).By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=14 µM for dimethylallyl diphosphate (in metal-free EDTA buffer)1 Publication
  2. KM=40 µM for L-tryptophan (in metal-free EDTA buffer)1 Publication
  3. KM=8 µM for dimethylallyl diphosphate (in the presence of 4 mM Ca2+)1 Publication
  4. KM=17 µM for L-tryptophan (in the presence of 4 mM Ca2+)1 Publication
  5. KM=8 µM for dimethylallyl diphosphate (in the presence of 4 mM Mg2+)1 Publication
  6. KM=12 µM for L-tryptophan (in the presence of 4 mM Mg2+)1 Publication
  1. Vmax=215 nmol/min/mg enzyme (in metal-free EDTA buffer)1 Publication
  2. Vmax=504 nmol/min/mg enzyme (in the presence of 4 mM Ca2+)1 Publication
  3. Vmax=455 nmol/min/mg enzyme (in the presence of 4 mM Mg2+)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei88L-tryptophanBy similarity1
Binding sitei99SubstrateBy similarity1
Binding sitei186SubstrateBy similarity1
Binding sitei188SubstrateBy similarity1
Binding sitei190L-tryptophanBy similarity1
Binding sitei256L-tryptophanBy similarity1
Binding sitei269SubstrateBy similarity1
Binding sitei271SubstrateBy similarity1
Binding sitei273SubstrateBy similarity1
Binding sitei355SubstrateBy similarity1
Binding sitei357SubstrateBy similarity1
Binding sitei421SubstrateBy similarity1
Binding sitei425SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processAlkaloid metabolism

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q12594

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00327

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M77.004

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tryptophan dimethylallyltransferase1 Publication (EC:2.5.1.342 Publications)
Alternative name(s):
4-dimethylallyltryptophan synthase1 Publication
Short name:
DMATS1 Publication
All-trans-hexaprenyl-diphosphate synthaseCurated
L-tryptophan dimethylallyl transferaseCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:dmaW1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiClaviceps fusiformis (Ergot fungus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri40602 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesClavicipitaceaeClaviceps

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001813631 – 455Tryptophan dimethylallyltransferaseAdd BLAST455

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q12594

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q12594

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni79 – 80L-tryptophan bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Conserved Domains Database

More...
CDDi
cd13929, PT-DMATS_CymD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR033964, Aro_prenylTrfase
IPR017795, Aro_prenylTrfase_DMATS
IPR012148, DMATS-type_fun
IPR017796, Trp_dimethylallylTrfase

The PANTHER Classification System

More...
PANTHERi
PTHR40627, PTHR40627, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF11991, Trp_DMAT, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000509, Trp_DMAT, 1 hit

Structure-Function Linkage Database

More...
SFLDi
SFLDS00036, Aromatic_Prenyltransferase, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03429, arom_pren_DMATS, 1 hit
TIGR03430, trp_dimet_allyl, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q12594-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMTKAPATAV YDTLSLLFDF PNQEQRLWWH SIAPMFAAML DTAGHNVHDQ
60 70 80 90 100
YRHLGIFKKH IIPFLGVYPA QGKHTWPSVL TRYGIPFELS LNCLDSVVRY
110 120 130 140 150
TFEPTTEHTG TGDDSYNAFA ILECIQKLVR IQPGIDMEWF SYFRNELVLN
160 170 180 190 200
ATESARLGRN DSVNQQPIRT QNKLALDLKG DRFALKVYLY PHLKSIATGV
210 220 230 240 250
SSHDLIFNSV RKLSQKHTSI QPSFNVLCDY VASRNDPDSN AAEAEAGVPA
260 270 280 290 300
SALRARLLSC DLVDPSKSRI KIYLLEQTVS LTAMEDLWTL GGRRTDSSTL
310 320 330 340 350
NGLDMMRELW HLLQIPSGFM KYPESDLKLG EVPDEQLPSM VHYALHPDQP
360 370 380 390 400
MPEPQVYFTV FGMSDAGITN ALATFFSRHG WYEMAKKYRV FLEGSFPNHD
410 420 430 440 450
FESLNYLHTY VSFSYRKNKP YLSVYLHSFE TGQWPAFSDD PTAFNAFKRC

DLSLT
Length:455
Mass (Da):51,858
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA913F8E60EBBEB63
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L39640 Genomic DNA Translation: AAC18893.1
EU006773 Genomic DNA Translation: ABV57826.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39640 Genomic DNA Translation: AAC18893.1
EU006773 Genomic DNA Translation: ABV57826.1

3D structure databases

SMRiQ12594
ModBaseiSearch...

Protein family/group databases

MEROPSiM77.004

Proteomic databases

PRIDEiQ12594

Enzyme and pathway databases

UniPathwayiUPA00327
SABIO-RKiQ12594

Family and domain databases

CDDicd13929, PT-DMATS_CymD, 1 hit
InterProiView protein in InterPro
IPR033964, Aro_prenylTrfase
IPR017795, Aro_prenylTrfase_DMATS
IPR012148, DMATS-type_fun
IPR017796, Trp_dimethylallylTrfase
PANTHERiPTHR40627, PTHR40627, 1 hit
PfamiView protein in Pfam
PF11991, Trp_DMAT, 1 hit
PIRSFiPIRSF000509, Trp_DMAT, 1 hit
SFLDiSFLDS00036, Aromatic_Prenyltransferase, 1 hit
TIGRFAMsiTIGR03429, arom_pren_DMATS, 1 hit
TIGR03430, trp_dimet_allyl, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDMAW_CLAFS
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q12594
Secondary accession number(s): A8C7S2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1996
Last modified: December 11, 2019
This is version 70 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again