H6VLG5 · KSL2_SALMI
- ProteinEnt-13-epi-manoyl oxide synthase KSL2, chloroplastic
- GeneKSL2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids811 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Involved in diterpenoid biosynthesis (PubMed:26077765).
Catalyzes the conversion of ent-8alpha-hydroxylabd-13-en-15-yl diphosphate to ent-13-epi-manoyl oxide (PubMed:26077765).
Catalyzes the conversion of ent-8alpha-hydroxylabd-13-en-15-yl diphosphate to ent-13-epi-manoyl oxide (PubMed:26077765).
Catalytic activity
- ent-8alpha-hydroxylabd-13-en-15-yl diphosphate = diphosphate + ent-13-epi-manoyl oxideThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 3 Mg2+ ions per subunit.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 550 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 550 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 554 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 554 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 694 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 702 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | magnesium ion binding | |
Molecular Function | terpene synthase activity | |
Biological Process | gibberellin biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEnt-13-epi-manoyl oxide synthase KSL2, chloroplastic
- 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 accessionH6VLG5
- Secondary accessions
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-49 | Chloroplast | ||||
Sequence: MALPLSTCLLFHPKESRSRRFCFSPASAASLKSGLHSATSAKIASMPTC | ||||||
Chain | PRO_0000449932 | 50-811 | Ent-13-epi-manoyl oxide synthase KSL2, chloroplastic | |||
Sequence: FEQTRGRIAKLFHKDELSVSTYDTAWVAMVPSPTSLEEPCFPDCLNWLLENQCHDGSWARPHHHPLLKKDVLSSTLACILALKKWGVGEEQIKRGLHFLELNFASATDKCQITPMGFDIIFPAMLDYARGFSLNLRLDPTTFNDLMHKRDLELKRSNRNYSSETETYWAYIAEGMGELQNWESVMKYQRRNGSLFNCPSTTAAAFIALRNSDCLNYLHLALKKFGNAVSAVYPLDIYSQLCTVDNLERLGISQYFSTEIQNVLDETYRCWMQGNEEIFMDASTCALAFRTLRLNGYDVTSDPVTKILQECFSSSFRGNMTDINTTLELYRASELVLYPDERDLEKQNLRLKLLLEQELSSGLIQSCQLGRSINVLLISQVNQAIEYPFYAIMDRVAKRKSIEIYNFDNTRILKTSYCSPNFGNEDFHFLSIEDFNRCQAAHREELGELERWVVENRLDELKFARSKSAYCYFSAAATFFAPELLDARLSWAKNGVLTTVIDDFFDVGGSVEELKNLIQLVELWDVDICTECYSHNVQIIFSALRRTICEIGDKAFKLQGRCITNHIIAIWLDLLNSMMRETEWARDNFVPTIDEYMSNAHVSFALGPIVLPALYLVGPKLSEDMVNHSEYHNLFKLMSTCGRLLNDIHGYERELKDGKLNALSLYIINHGGEVSKEAAIWEMKSWIETQRRELLRLVLEGKKSVLPKPCRELFWHMCSVVHLFYSKGDGFTSQDLIQLVNTIIHQPILLNDQTGAGLSKLHD |
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 550-554 | DDXXD motif | ||||
Sequence: DDFFD |
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.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length811
- Mass (Da)92,639
- Last updated2020-06-17 v2
- Checksum50DFEC5AE912028B
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 594 | in Ref. 1; AHJ59325 | ||||
Sequence: R → C | ||||||
Sequence conflict | 672 | in Ref. 1; AHJ59325 | ||||
Sequence: D → E | ||||||
Sequence conflict | 811 | in Ref. 1; AHJ59325 | ||||
Sequence: D → G |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KC814643 EMBL· GenBank· DDBJ | AHJ59325.1 EMBL· GenBank· DDBJ | mRNA | ||
JN831119 EMBL· GenBank· DDBJ | AEZ55689.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |