Q947C4 · TPSD1_GINBI
- ProteinBifunctional levopimaradiene synthase, chloroplastic
- GeneLPS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids873 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the initial cyclization step in the biosynthesis of ginkgolides, a structurally unique family of diterpenoids that are highly specific platelet-activating-factor receptor antagonists. Bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate (GGPP) to levopimaradiene.
Catalytic activity
- (2E,6E,10E)-geranylgeranyl diphosphate = +-copalyl diphosphate
Cofactor
Note: Binds 3 Mg2+ ions per subunit.
pH Dependence
Optimum pH is 7.2.
Pathway
Terpene metabolism; ginkgolide biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 271 | substrate | ||||
Sequence: K | ||||||
Binding site | 405 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 407 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 492 | substrate | ||||
Sequence: K | ||||||
Binding site | 624 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 624 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 628 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 628 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 769 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 773 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 777 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | copalyl diphosphate synthase activity | |
Molecular Function | levopimaradiene synthase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | terpene synthase activity | |
Biological Process | diterpenoid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional levopimaradiene synthase, chloroplastic
- Alternative names
Including 2 domains:
- Recommended nameLevopimaradiene synthase
- EC number
- Recommended nameCopalyl diphosphate synthase
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Ginkgoidae > Ginkgoales > Ginkgoaceae > Ginkgo
Accessions
- Primary accessionQ947C4
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-59 | Chloroplast | ||||
Sequence: MAGVLFANLPCSLQLSPKVPFRQSTNILIPFHKRSSFGFNAQHCVRSHLRLRWNCVGIH | ||||||
Chain | PRO_0000348950 | 60-873 | Bifunctional levopimaradiene synthase, chloroplastic | |||
Sequence: ASAAETRPDQLPQEERFVSRLNADYHPAVWKDDFIDSLTSPNSHATSKSSVDETINKRIQTLVKEIQCMFQSMGDGETNPSAYDTAWVARIPSIDGSGAPQFPQTLQWILNNQLPDGSWGEECIFLAYDRVLNTLACLLTLKIWNKGDIQVQKGVEFVRKHMEEMKDEADNHRPSGFEVVFPAMLDEAKSLGLDLPYHLPFISQIHQKRQKKLQKIPLNVLHNHQTALLYSLEGLQDVVDWQEITNLQSRDGSFLSSPASTACVFMHTQNKRCLHFLNFVLSKFGDYVPCHYPLDLFERLWAVDTVERLGIDRYFKKEIKESLDYVYRYWDAERGVGWARCNPIPDVDDTAMGLRILRLHGYNVSSDVLENFRDEKGDFFCFAGQTQIGVTDNLNLYRCSQVCFPGEKIMEEAKTFTTNHLQNALAKNNAFDKWAVKKDLPGEVEYAIKYPWHRSMPRLEARSYIEQFGSNDVWLGKTVYKMLYVSNEKYLELAKLDFNMVQALHQKETQHIVSWWRESGFNDLTFTRQRPVEMYFSVAVSMFEPEFAACRIAYAKTSCLAVILDDLYDTHGSLDDLKLFSEAVRRWDISVLDSVRDNQLKVCFLGLYNTVNGFGKDGLKEQGRDVLGYLRKVWEGLLASYTKEAEWSAAKYVPTFNEYVENAKVSIALATVVLNSIFFTGELLPDYILQQVDLRSKFLHLVSLTGRLINDTKTYQAERNRGELVSSVQCYMRENPECTEEEALSHVYGIIDNALKELNWELANPASNAPLCVRRLLFNTARVMQLFYMYRDGFGISDKEMKDHVSRTLFDPVA |
Expression
Tissue specificity
Expressed in roots.
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 405-408 | DXDD motif | ||||
Sequence: DVDD | ||||||
Motif | 624-628 | DDXXD motif | ||||
Sequence: DDLYD |
Domain
The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity in the class II active site relevant for the cyclization of GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity in the class I active site, presumably through binding to Mg2+.
Sequence similarities
Belongs to the terpene synthase family. Tpsd subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length873
- Mass (Da)100,290
- Last updated2001-12-01 v1
- ChecksumF2C980BB19F9931E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF331704 EMBL· GenBank· DDBJ | AAL09965.1 EMBL· GenBank· DDBJ | mRNA | ||
AY574248 EMBL· GenBank· DDBJ | AAS89668.1 EMBL· GenBank· DDBJ | Genomic DNA |