G8H5N1 · TS14B_SOLHA

Function

function

Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683).
Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into +-thujopsene, beta-bisabolene, alpha-cederene, beta-acoradiene, (E)-gamma-bisabolene, (Z)-alpha-bisabolene, (Z)-beta-farnesene and (E)-beta-farnesene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-gamma-bisabolene, (E)-alpha-bisabolene, (E)-beta-farnesene, (Z)-beta-farnesene, beta-bisabolene, beta-acoradiene and alpha-acoradiene (PubMed:21818683).
Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene and terpinolene (PubMed:21818683).

Catalytic activity

  • (2E,6E)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate
    This reaction proceeds in the forward direction.
    EC:4.2.3.59 (UniProtKB | ENZYME | Rhea)
  • (2Z,6Z)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate
    This reaction proceeds in the forward direction.
  • (2Z,6Z)-farnesyl diphosphate = (E)-alpha-bisabolene + diphosphate
    This reaction proceeds in the forward direction.
  • (2Z,6Z)-farnesyl diphosphate = (Z)-beta-farnesene + diphosphate
    This reaction proceeds in the forward direction.
  • (2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate
    This reaction proceeds in the forward direction.
    EC:4.2.3.47 (UniProtKB | ENZYME | Rhea)
  • (2E,6E)-farnesyl diphosphate = +-thujopsene + diphosphate
    This reaction proceeds in the forward direction.
    EC:4.2.3.79 (UniProtKB | ENZYME | Rhea)
  • (2Z,6Z)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate
    This reaction proceeds in the forward direction.
  • (2E,6E)-farnesyl diphosphate = (Z)-beta-farnesene + diphosphate
    This reaction proceeds in the forward direction.
  • (2Z,6Z)-farnesyl diphosphate = beta-acoradiene + diphosphate
    This reaction proceeds in the forward direction.
  • (2Z,6Z)-farnesyl diphosphate = alpha-acoradiene + diphosphate
    This reaction proceeds in the forward direction.
  • (2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate
    This reaction proceeds in the forward direction.
  • (2E,6E)-farnesyl diphosphate = --alpha-cedrene + diphosphate
    This reaction proceeds in the forward direction.
  • (2E,6E)-farnesyl diphosphate = beta-bisabolene + diphosphate
    This reaction proceeds in the forward direction.
  • (2E,6E)-farnesyl diphosphate = beta-acoradiene + diphosphate
    This reaction proceeds in the forward direction.
  • (2Z,6Z)-farnesyl diphosphate = --alpha-cedrene + diphosphate
    This reaction proceeds in the forward direction.
  • (2E)-geranyl diphosphate = diphosphate + terpinolene
    This reaction proceeds in the forward direction.
    EC:4.2.3.113 (UniProtKB | ENZYME | Rhea)
  • (2E)-geranyl diphosphate = diphosphate + limonene
    This reaction proceeds in the forward direction.
  • (2E)-geranyl diphosphate = beta-myrcene + diphosphate
    This reaction proceeds in the forward direction.
    EC:4.2.3.15 (UniProtKB | ENZYME | Rhea)

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.

TypeIDPosition(s)Description
Binding site305Mg2+ 1 (UniProtKB | ChEBI)
Binding site305Mg2+ 2 (UniProtKB | ChEBI)
Binding site309Mg2+ 1 (UniProtKB | ChEBI)
Binding site309Mg2+ 2 (UniProtKB | ChEBI)
Binding site449Mg2+ 3 (UniProtKB | ChEBI)
Binding site457Mg2+ 3 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionhydrolase activity
Molecular Functionmagnesium ion binding
Molecular Functionterpene synthase activity
Biological Processditerpenoid biosynthetic process
Biological Processterpenoid biosynthetic process

Keywords

Enzyme and pathway databases

Community curation (1)

Sesquiterpene synthase which can use either (Z,Z)-FPP or (E,E)-FPP as a substrate. In the presence of (Z,Z)-FPP the enzyme produces predominantly (Z)-beta-farnesene, alpha- and beta-acoradiene and alpha- and gamma-bisabolenes, while when assayed with (E,E)-FPP alpha-cederene, (Z)-thujopsene, beta-farnesene, beta-acoradiene and beta-bisabolene are produced.

Names & Taxonomy

Protein names

  • Recommended name
    Sesquiterpene synthase 14b
  • Short names
    ShTPS14b
  • Alternative names
    • (+)-thujopsene synthase TPS14b
      (EC:4.2.3.79
      ) . EC:4.2.3.79 (UniProtKB | ENZYME | Rhea)
    • (E)-alpha-bisabolene synthase TPS14b
      (EC:4.2.3.-
      ) . EC:4.2.3.- (UniProtKB | ENZYME | Rhea)
    • (E)-beta-farnesene synthase TPS14b
      (EC:4.2.3.47
      ) . EC:4.2.3.47 (UniProtKB | ENZYME | Rhea)
    • (E)-gamma-bisabolene synthase TPS14b
      (EC:4.2.3.59
      ) . EC:4.2.3.59 (UniProtKB | ENZYME | Rhea)
    • (Z)-beta-farnesene synthase TPS14b
      (EC:4.2.3.-
      ) . EC:4.2.3.- (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      TPS14b
Community curation (1)

Organism names

  • Taxonomic identifier
  • Strain
    • cv. PI126449
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Solanales > Solanaceae > Solanoideae > Solaneae > Solanum > Solanum subgen. Lycopersicon

Accessions

  • Primary accession
    G8H5N1

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004546851-554Sesquiterpene synthase 14b

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif305-309DDXXD 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. Tpsa subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    554
  • Mass (Da)
    65,036
  • Last updated
    2012-01-25 v1
  • Checksum
    863D6F4D56FD8FE0
MNQLAMVNTTITRPLANYHSSVWGNYFLSYTPQLTEISSQEKRELEELKEKVRQMLVETPDNSTQKLVLIDTIQRLGVAYHFENHIKISIQNIFDEFEKNKNKDNDDDLCVVALRFRLVRGQRHYMSSDVFTRFTNDDGKFKETLTKDVQGLLNLYEATHLRVHGEEILEEALSFTVTHLKSMSPKLDNSLKAQVSEALFQPIHTNIPRVVARKYIRIYENIESHDDLLLKFAKLDFHILQKMHQRELSELTRWWKDLDHSNKYPYARDKLVECYFWAIGVYFGPQYKRARRTLTKLIVIITITDDLYDAYATYDELVPYTNAVERCEISAMHSISPYMRPLYQVFLDYFDEMEEELTKDGKAHYVYYAKIETNKWIKSYLKEAEWLKNDIIPKCEEYKRNATITISNQMNLITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFIECYVKEYRASKQEAYVEARRQITNAWKDINTDYLHATQVPTFVLEPALNLSRLVDILQEDDFTDSQNFLKDTITLLFVDSVNSTSCG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JN402392
EMBL· GenBank· DDBJ
AEM23829.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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