A0A1W6GW18 · STPS3_SALMI
- Protein(-)-5-epieremophilene synthase STPS3
- GeneSTPS3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids546 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Sesquiterpene synthase that catalyzes the conversion of farnesyl diphosphate to --5-epi-eremophilene.
Catalytic activity
- (2E,6E)-farnesyl diphosphate = --5-epi-eremophilene + diphosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 3 Mg2+ ions per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
10.44 μM | farnesyl diphosphate |
kcat is 1.53 sec-1 with farnesyl diphosphate as substrate.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 299 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 299 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 303 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 303 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 442 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 446 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 450 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | magnesium ion binding | |
Molecular Function | terpene synthase activity | |
Biological Process | diterpenoid biosynthetic process | |
Biological Process | sesquiterpenoid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name(-)-5-epieremophilene synthase STPS3
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Lamiales > Lamiaceae > Nepetoideae > Mentheae > Salviinae > Salvia > Salvia incertae sedis
Accessions
- Primary accessionA0A1W6GW18
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000447714 | 1-546 | --5-epieremophilene synthase STPS3 | |||
Sequence: MATTQVEIQRPIANFSPSLWGDQFIKNDSGAKAAEKHCKAVEELKKEVMNMITAAESNLVEAMNLIDTLERLGISYHFEKEIDQKLNHFFSLNTDYSDESYDLYTVSLHFRLFRQHGHRISSDIFGRWIDESGKFKEGLKTDGKGLLSLYEASYLRTRGETILDDALEFATATLNSIAPHLESPLSKQVVHALIQPLHYGNPRIEAHNFISIYEENQDKNEFLLKFAKLDYNLLQMLHKEELHEVSRWWKELDLVSKLPYARDRVVECFFWAMGVYHEPQYSRARIMLTKTITMTSIIDDTYDAYGVIEELDIFTEAIERWNIEEMDRLPEYVKPFYKALLELYEQFEEELAEEGRSYAAHYAIESLKELVRSYHVEAKWFIQGYLPPFEEYLKNALITCTYCYHTTTSLLGVESAVEEDFQWLAKKPKMLVAGLLICRVIDDIATYEVEKERGQSATGIESYMRDNNATIEEAVAKFFEIATDAWKDINEECLMPSPYSRDVLMRILNLERIIDVTYKGNEDGYTQPEKVLKPHIIALFVDPIKM |
Expression
Tissue specificity
Highly expressed in flowers and at lower levels in leaves.
Induction
Induced by abscisic acid (ABA).
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 299-303 | DDXXD motif | ||||
Sequence: DDTYD |
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 statusComplete
- Length546
- Mass (Da)63,501
- Last updated2017-07-05 v1
- ChecksumA725FF1A69E5BAD7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KY432514 EMBL· GenBank· DDBJ | ARM19969.1 EMBL· GenBank· DDBJ | mRNA |