A7IZZ1 · TPS1_CANSA
- Protein(-)-limonene synthase TPS1, chloroplastic
- GeneTPS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids623 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in monoterpene (C10) olefins biosynthesis, constituants of cannabinoids and terpenoids-rich resins (PubMed:31138625, Ref.1). Catalyzes mainly the conversion of (2E)-geranyl diphosphate to --limonene, and produces also minor products such as +-limonene, +-alpha-pinene, terpinolene, +-beta-pinene and beta-myrcene (PubMed:31138625, Ref.1).
Catalytic activity
- (2E)-geranyl diphosphate = (4S)-limonene + diphosphateThis reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 3 Mg2+ or Mn2+ ions per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
6.8 μM | Geranyl pyrophosphate |
pH Dependence
Optimum pH is 6.5.
Temperature Dependence
Optimum temperature is 40 degrees Celsius.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Terpene metabolism; (4S)-limonene biosynthesis; (4S)-limonene from geranyl diphosphate: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 337 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 374 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 374 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 374 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 378 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 378 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 378 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 516 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 519 | (2E)-geranyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 519 | Mg2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 523 | Mg2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 527 | Mg2+ 3 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | (4S)-limonene synthase activity | |
Molecular Function | (R)-limonene synthase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | myrcene synthase activity | |
Biological Process | diterpenoid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name(-)-limonene synthase TPS1, chloroplastic
- EC number
- Short names(-)-(4S)-limonene synthase
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Cannabaceae > Cannabis
Accessions
- Primary accessionA7IZZ1
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-60 | Chloroplast | |||
Chain | PRO_0000363060 | 61-623 | --limonene synthase TPS1, chloroplastic | ||
Expression
Tissue specificity
Trichome.
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 29-52 | Disordered | |||
Motif | 374-378 | DDXXD motif | |||
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.
- Length623
- Mass (Da)72,516
- Last updated2024-10-02 v2
- ChecksumE0D56B401C04B9ED
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 58 | in Ref. 1; ABI21837 | |||
Sequence conflict | 161 | in Ref. 1; ABI21837 and 2; QCY41294 | |||
Sequence conflict | 166 | in Ref. 2; QCY41294 | |||
Sequence conflict | 167 | in Ref. 1; ABI21837 | |||
Sequence conflict | 585-586 | in Ref. 2; QCY41294 | |||
Sequence conflict | 586 | in Ref. 1; ABI21837 | |||
Sequence conflict | 594-595 | in Ref. 2; QCY41294 | |||
Sequence conflict | 595 | in Ref. 1; ABI21837 | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ839404 EMBL· GenBank· DDBJ | ABI21837.1 EMBL· GenBank· DDBJ | mRNA | ||
MK801766 EMBL· GenBank· DDBJ | QCY41294.1 EMBL· GenBank· DDBJ | mRNA | ||
JAATIP010000065 EMBL· GenBank· DDBJ | KAF4380280.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UZAU01000409 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |