A0A1W6GW18 · STPS3_SALMI

Function

function

Sesquiterpene synthase that catalyzes the conversion of farnesyl diphosphate to --5-epi-eremophilene.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 3 Mg2+ ions per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
10.44 μMfarnesyl diphosphate
kcat is 1.53 sec-1 with farnesyl diphosphate as substrate.

Pathway

Secondary metabolite biosynthesis; terpenoid biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site299Mg2+ 1 (UniProtKB | ChEBI)
Binding site299Mg2+ 2 (UniProtKB | ChEBI)
Binding site303Mg2+ 1 (UniProtKB | ChEBI)
Binding site303Mg2+ 2 (UniProtKB | ChEBI)
Binding site442Mg2+ 3 (UniProtKB | ChEBI)
Binding site446Mg2+ 3 (UniProtKB | ChEBI)
Binding site450Mg2+ 3 (UniProtKB | ChEBI)

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    (-)-5-epieremophilene synthase STPS3
  • EC number
  • Alternative names
    • Sesquiterpene synthase 3
      (SmSTPS3
      )

Gene names

    • Name
      STPS3

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Lamiales > Lamiaceae > Nepetoideae > Mentheae > Salviinae > Salvia > Salvia incertae sedis

Accessions

  • Primary accession
    A0A1W6GW18

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004477141-546--5-epieremophilene synthase STPS3

Expression

Tissue specificity

Highly expressed in flowers and at lower levels in leaves.

Induction

Induced by abscisic acid (ABA).

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif299-303DDXXD 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
    546
  • Mass (Da)
    63,501
  • Last updated
    2017-07-05 v1
  • Checksum
    A725FF1A69E5BAD7
MATTQVEIQRPIANFSPSLWGDQFIKNDSGAKAAEKHCKAVEELKKEVMNMITAAESNLVEAMNLIDTLERLGISYHFEKEIDQKLNHFFSLNTDYSDESYDLYTVSLHFRLFRQHGHRISSDIFGRWIDESGKFKEGLKTDGKGLLSLYEASYLRTRGETILDDALEFATATLNSIAPHLESPLSKQVVHALIQPLHYGNPRIEAHNFISIYEENQDKNEFLLKFAKLDYNLLQMLHKEELHEVSRWWKELDLVSKLPYARDRVVECFFWAMGVYHEPQYSRARIMLTKTITMTSIIDDTYDAYGVIEELDIFTEAIERWNIEEMDRLPEYVKPFYKALLELYEQFEEELAEEGRSYAAHYAIESLKELVRSYHVEAKWFIQGYLPPFEEYLKNALITCTYCYHTTTSLLGVESAVEEDFQWLAKKPKMLVAGLLICRVIDDIATYEVEKERGQSATGIESYMRDNNATIEEAVAKFFEIATDAWKDINEECLMPSPYSRDVLMRILNLERIIDVTYKGNEDGYTQPEKVLKPHIIALFVDPIKM

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KY432514
EMBL· GenBank· DDBJ
ARM19969.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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