Q1XBU5 · TPS5_SOLLC
- Protein(R)-linalool synthase TPS5, chloroplastic
- GeneTPS5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids609 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Involved in monoterpene (C10) biosynthesis in glandular trichomes (PubMed:17440821).
Converts geranyl diphosphate to linalool in glandular trichomes in response to jasmonate (JA) (PubMed:17440821).
Can convert farnesyl diphosphate to nerolidol in vitro (PubMed:17440821).
Converts geranyl diphosphate to linalool in glandular trichomes in response to jasmonate (JA) (PubMed:17440821).
Can convert farnesyl diphosphate to nerolidol in vitro (PubMed:17440821).
Catalytic activity
- (2E)-geranyl diphosphate + H2O = (R)-linalool + diphosphate
- (2E,6E)-farnesyl diphosphate + H2O = (6E)-nerolidol + diphosphate
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 3 Mg2+ or Mn2+ ions per subunit.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 325 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 362 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 362 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 362 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 366 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 366 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 366 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 503 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 506 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 506 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 510 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 514 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | magnesium ion binding | |
Molecular Function | R-linalool synthase activity | |
Molecular Function | terpene synthase activity | |
Biological Process | diterpenoid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name(R)-linalool synthase TPS5, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Solanales > Solanaceae > Solanoideae > Solaneae > Solanum > Solanum subgen. Lycopersicon
Accessions
- Primary accessionQ1XBU5
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-42 | Chloroplast | ||||
Sequence: MVSILSNIGMMVVTFKRPSLFTSLRRRSANNIIITKHSHPIS | ||||||
Chain | PRO_0000447554 | 43-609 | (R)-linalool synthase TPS5, chloroplastic | |||
Sequence: TTRRSGNYKPTMWDFQFIQSLHNPYEGDKYMKRLNKLKKEVKKMMMTVEGSHDEELEKLELIDNLERLGVSYHFKDEIMQIMRSINININIAPPDSLYTTALKFRLLRQHGFHISQDILNDFKDENGNLKQSICKDTKDILNSSKDEHDNLKQSTCNNTKGLLKLYEASFLSIENESFLRNTTKSTLAHLMRYVDQNRCGEEDNMIVELVVHALELPRHWMVPRLETRWYISIYERMSNANPLLLELAKLDFNIVQATHQQDLRILSRWWKNTGLAEKLPFSRDILVENMFWAVGALFEPQHSYFRRLITKVIVFISIIDDIYDVYGTLDELELFTLAIQRWDTKAMEQLPDYMKVCYLALINIINEVAYEVLKNHDINVLPYLTKSWADLCKSYLQEAKWYHNGYKPNLEEYMDNARISIGVPMVLVHSLFLVTNQITKEALDSLTNYPDIIRWSATIFRLNDDLGTSSDELKRGDVSKSIQCYMNEKGASEEEAIEHIEFLIQETWEAMNTAQSKNSPLSETFIEVAKNITKASHFMYLHSDVKSSISKILFEPIIISNVAFALK |
Proteomic databases
Expression
Tissue specificity
Highly expressed in young fruits and plant tops (PubMed:17440821).
Expressed in flower buds and trichomes of petioles and stems (PubMed:17440821).
Expressed at low levels in young leaves, stems, petioles, sepals and petals (PubMed:17440821).
Expressed in flower buds and trichomes of petioles and stems (PubMed:17440821).
Expressed at low levels in young leaves, stems, petioles, sepals and petals (PubMed:17440821).
Induction
Induced by spider mite feeding, wounding and jasmonate (JA).
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 362-366 | DDXXD motif | ||||
Sequence: DDIYD |
Domain
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+.
Sequence similarities
Belongs to the terpene synthase family. Tpsb subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length609
- Mass (Da)70,945
- Last updated2006-05-02 v1
- Checksum3BEAB8BC9DF30082
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY840091 EMBL· GenBank· DDBJ | AAX69063.1 EMBL· GenBank· DDBJ | mRNA | ||
JN408286 EMBL· GenBank· DDBJ | AEM05855.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM001064 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |