E9E766 · BTPSL_METAQ
- ProteinSesquiterpene synthase MAC_05714
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids349 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Terpene synthase that catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into sesquiterpenes which are important for fungi-environment interactions (PubMed:31239482).
Produces a mixture consisting of 8 sesquiterpenes including corvol ethers A and B, as well as traces of epizonarene, gamma-cadinene, delta-cadinene, alpha-cadinene, alpha-cadinol, and an unidentified sesquiterpene (PubMed:31239482).
Produces both corvol ether A and corvol ether B in similar concentrations (PubMed:31239482).
Produces a mixture consisting of 8 sesquiterpenes including corvol ethers A and B, as well as traces of epizonarene, gamma-cadinene, delta-cadinene, alpha-cadinene, alpha-cadinol, and an unidentified sesquiterpene (PubMed:31239482).
Produces both corvol ether A and corvol ether B in similar concentrations (PubMed:31239482).
Catalytic activity
- (2E,6E)-farnesyl diphosphate + H2O = +-corvol ether B + diphosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 3 Mg2+ ions per subunit.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 88 | Plays a critical role in the stabilization of intermediate cation | ||||
Sequence: F | ||||||
Binding site | 91 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 92 | Plays a critical role for substrate recognition | ||||
Sequence: D | ||||||
Binding site | 96 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 96 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 184 | substrate | ||||
Sequence: R | ||||||
Binding site | 230 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 234 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 238 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | lyase activity | |
Molecular Function | metal ion binding | |
Biological Process | isoprenoid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSesquiterpene synthase MAC_05714
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Metarhizium
Accessions
- Primary accessionE9E766
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451050 | 1-349 | Sesquiterpene synthase MAC_05714 | |||
Sequence: MEKQHLKSQIAALRVPTFNIAWPERRSPKADVVEERMMKWADHHKLLVNGEYRDRVIRTRYGLLAARCYPNAGEELLQAIADYFVWFFLADDLFVDRVEVVTDETIRNLTAMIDVLDRNVAREEPVFGELAWLDVCQRLRDLLQPEAFQRFAQGMRLWATTAALQILNHQRPKSVGIREYEAIRRHTSGLNPCTSLADAANKGSVQAHEFYQPDVQKLVLQTNNIVCWANDIQSLGMEIQQPGQFRNMVTIYIQQGQSLSEAVSTTTARVNNELSDFCKLADIVTAPSISDELRVYVDGLKYWIRGYMDWVVHDTERYADKFIASDADDRCVSTLNPSLLNRSSSSATE |
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 91-96 | DDXXXD motif | ||||
Sequence: DDLFVD |
Domain
The Asp-Asp-Xaa-Xaa-Xaa-Asp (DDXXXD) motif is important for the catalytic activity, presumably through binding to Mg2+.
Sequence similarities
Belongs to the terpene synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length349
- Mass (Da)39,947
- Last updated2011-04-05 v1
- Checksum08EEDA1CAB36CF2D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL698514 EMBL· GenBank· DDBJ | EFY88241.1 EMBL· GenBank· DDBJ | Genomic DNA |