A7IZZ1 · TPS1_CANSA

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

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 3 Mg2+ or Mn2+ ions per subunit.
K+ (UniProtKB | Rhea| CHEBI:29103 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
6.8 μMGeranyl 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.

TypeIDPosition(s)Description
Binding site337(2E)-geranyl diphosphate (UniProtKB | ChEBI)
Binding site374(2E)-geranyl diphosphate (UniProtKB | ChEBI)
Binding site374Mg2+ 1 (UniProtKB | ChEBI)
Binding site374Mg2+ 2 (UniProtKB | ChEBI)
Binding site378(2E)-geranyl diphosphate (UniProtKB | ChEBI)
Binding site378Mg2+ 1 (UniProtKB | ChEBI)
Binding site378Mg2+ 2 (UniProtKB | ChEBI)
Binding site516(2E)-geranyl diphosphate (UniProtKB | ChEBI)
Binding site519(2E)-geranyl diphosphate (UniProtKB | ChEBI)
Binding site519Mg2+ 3 (UniProtKB | ChEBI)
Binding site523Mg2+ 3 (UniProtKB | ChEBI)
Binding site527Mg2+ 3 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Function(4S)-limonene synthase activity
Molecular Function(R)-limonene synthase activity
Molecular Functionmagnesium ion binding
Molecular Functionmyrcene synthase activity
Biological Processditerpenoid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    (-)-limonene synthase TPS1, chloroplastic
  • EC number
  • Short names
    (-)-(4S)-limonene synthase
  • Alternative names
    • (+)-alpha-pinene synthase TPS1
      (EC:4.2.3.121
      ) . EC:4.2.3.121 (UniProtKB | ENZYME | Rhea)
    • (+)-beta-pinene synthase TPS1
      (EC:4.2.3.122
      ) . EC:4.2.3.122 (UniProtKB | ENZYME | Rhea)
    • (R)-limonene synthase
      (EC:4.2.3.20
      ) . EC:4.2.3.20 (UniProtKB | ENZYME | Rhea)
    • Myrcene synthase TPS1
      (EC:4.2.3.15
      ) . EC:4.2.3.15 (UniProtKB | ENZYME | Rhea)
    • Terpene synthase 1
      (CsTPS1
      )

Gene names

    • Name
      TPS1
    • Synonyms
      TPS14CT

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Skunk
    • cv. Black Lime
    • cv. Blackberry Kush
    • cv. Canna Tsu
    • cv. Cherry Chem
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Cannabaceae > Cannabis

Accessions

  • Primary accession
    A7IZZ1
  • Secondary accessions
    • A0A4Y5QVX4
    • A0A7J6GDG9
    • A0A803R1P5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

Type
IDPosition(s)Description
Transit peptide1-60Chloroplast
ChainPRO_000036306061-623--limonene synthase TPS1, chloroplastic

Expression

Tissue specificity

Trichome.

Structure

3D structure databases

Family & Domains

Features

Showing features for region, motif.

Type
IDPosition(s)Description
Region29-52Disordered
Motif374-378DDXXD 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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    623
  • Mass (Da)
    72,516
  • Last updated
    2024-10-02 v2
  • Checksum
    E0D56B401C04B9ED
MQCIAFHQFASSSSLPIWSSIDNRFTPKTSITSISKPKPKLKSKSNLKSRSRSSTCYPIQCTVVDNPSSTITNNSDRRSANYGPPIWSFDFVQSLPIQYKGESYTSRLNKLEKDVKRMLIGVENSLAQLELIDTIQRLGISYRFENEIISILKEKFTNNNNNPNPINYDLYATALQFRLLRQYGFEVPQEIFNNFKNHKTGEFKANISNDIMGALGLYEASFHGKKGESILEEARIFTTKCLKKYKLMSSSNNNNMTLISLLVNHALEMPLQWRITRSEAKWFIEEIYERKQDMNPTLLEFAKLDFNMLQSTYQEELKVLSRWWKDSKLGEKLPFVRDRLVECFLWQVGVRFEPQFSYFRIMDTKLYVLLTIIDDMHDIYGTLEELQLFTNALQRWDLKELDKLPDYMKTAFYFTYNFTNELAFDVLQEHGFVHIEYFKKLMVELCKHHLQEAKWFYSGYKPTLQEYVENGWLSVGGQVILMHAYFAFTNPVTKEALECLKDGHPNIVRHASIILRLADDLGTLSDELKRGDVPKSIQCYMHDTGASEDEAREHIKYLISESWKEMNNEDGNINSFFSNEFVQVKQNLGRASQMIYQYGDGHASQNNLSKERVLGLIITPIPM

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict58in Ref. 1; ABI21837
Sequence conflict161in Ref. 1; ABI21837 and 2; QCY41294
Sequence conflict166in Ref. 2; QCY41294
Sequence conflict167in Ref. 1; ABI21837
Sequence conflict585-586in Ref. 2; QCY41294
Sequence conflict586in Ref. 1; ABI21837
Sequence conflict594-595in Ref. 2; QCY41294
Sequence conflict595in Ref. 1; ABI21837

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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.

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