A0A0P0ZEM1 · STLSS_EMEVA
- ProteinStellatatriene synthase
- GeneStl-SS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids714 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Multifunctional diterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene stellatic acid (PubMed:26351860).
The first step in the pathway is performed by the stellatatriene synthase that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and then converting GGDP into stellata-2,6,19-triene (PubMed:26351860).
The cytochrome P450 monooxygenase Stl-P450 then catalyzes three successive oxidation reactions on the C-20 methyl group to generate the carboxylic acid of stellatic acid (PubMed:26351860).
The first step in the pathway is performed by the stellatatriene synthase that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and then converting GGDP into stellata-2,6,19-triene (PubMed:26351860).
The cytochrome P450 monooxygenase Stl-P450 then catalyzes three successive oxidation reactions on the C-20 methyl group to generate the carboxylic acid of stellatic acid (PubMed:26351860).
Catalytic activity
- dimethylallyl diphosphate + 4 isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 4 diphosphateThis reaction proceeds in the forward direction.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 92 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | substrate | ||||
Sequence: D | ||||||
Binding site | 96 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 96 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 96 | substrate | ||||
Sequence: D | ||||||
Binding site | 179-182 | substrate | ||||
Sequence: RIQD | ||||||
Binding site | 227-231 | substrate | ||||
Sequence: SWEKE | ||||||
Binding site | 316-317 | substrate | ||||
Sequence: RY | ||||||
Binding site | 434 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 437 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 466 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 473 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 473 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 477 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 477 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 482 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 483 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 560 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 561 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 596 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 603 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 613 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 623 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 632-633 | substrate | ||||
Sequence: MQ |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | lyase activity | |
Molecular Function | metal ion binding | |
Molecular Function | prenyltransferase activity | |
Biological Process | alcohol biosynthetic process | |
Biological Process | ketone biosynthetic process | |
Biological Process | mycotoxin biosynthetic process | |
Biological Process | terpenoid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStellatatriene synthase
- Short namesSS
- Alternative names
Including 2 domains:
- Recommended nameGeranylgeranyl diphosphate synthase
- EC number
- Short namesGGDP synthase ; GGS
- Recommended namestellata-2,6,19-trien synthase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionA0A0P0ZEM1
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452514 | 1-714 | Stellatatriene synthase | |||
Sequence: MEYKFSTVVDPGTYETHGLCEGYEVRYHKNAELEDIGCLRCQEHWRQSVGPLGAFKGTLGNPFNLLSLVIPECLPDRLSIVGFANELAFIHDDVTDIVQYGDAHNNDFKEAFNSMATTGSMENAASGKRALQAYIAREMVRIDKERAIPTIKAWAKFVDYGGRQETTRFTSEKEYTEYRIQDIGLWFWYGLLSFAMALDVPEHEREMCHEVCRTAYVQIMLVHDLASWEKEKLNAAALGKDVITNIIFVLMEEHGISEEEAKERCRETAKTLAADYLKIVEEYKARDDISLDSRKYIESWLYTISGNTVWSFICPRYNSSGSFSDHQLELMKNGVPKDPASGSTNGTSNGTSNGTSHVAVNGNGHVTNDDLSANGIKTDGELLSAITMEHLKNRNSFKLGDHDQEVKSLHGHGQALDPRVLQAPYEYITALPSKGLREQAIDALNVWFRVPTAKLEIIKSITTILHNASLMLDDVEDGSELRRGKPATHNIFGLGQTINSANYQLVRALQELQKLGDARSLLVFTEELHNLYVGQSMDLYWTSNLVCPSMHEYFQMIEHKTGGLFRLFGRLMAVHSTNPVQVDLTDFTNHLGRYFQTRDDYQNLVSAEYTKQKGFCEDFEEGKFSLPMIHLMQTMPDNLVLRNVWTQRRVNGTATHGQKQTILNLMKEAGTLKFTQDSLGVLYSDVEKSVAELESKFGIENFQLRLIMELLKTG |
Interaction
Subunit
Hexamer.
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-325 | stellata-2,6,19-trien synthase | ||||
Sequence: MEYKFSTVVDPGTYETHGLCEGYEVRYHKNAELEDIGCLRCQEHWRQSVGPLGAFKGTLGNPFNLLSLVIPECLPDRLSIVGFANELAFIHDDVTDIVQYGDAHNNDFKEAFNSMATTGSMENAASGKRALQAYIAREMVRIDKERAIPTIKAWAKFVDYGGRQETTRFTSEKEYTEYRIQDIGLWFWYGLLSFAMALDVPEHEREMCHEVCRTAYVQIMLVHDLASWEKEKLNAAALGKDVITNIIFVLMEEHGISEEEAKERCRETAKTLAADYLKIVEEYKARDDISLDSRKYIESWLYTISGNTVWSFICPRYNSSGSFSD | ||||||
Motif | 92-96 | DDXXD motif 1 | ||||
Sequence: DDVTD | ||||||
Motif | 276-284 | NSE motif | ||||
Sequence: YLKIVEEYK | ||||||
Region | 326-713 | Geranylgeranyl diphosphate synthase | ||||
Sequence: HQLELMKNGVPKDPASGSTNGTSNGTSNGTSHVAVNGNGHVTNDDLSANGIKTDGELLSAITMEHLKNRNSFKLGDHDQEVKSLHGHGQALDPRVLQAPYEYITALPSKGLREQAIDALNVWFRVPTAKLEIIKSITTILHNASLMLDDVEDGSELRRGKPATHNIFGLGQTINSANYQLVRALQELQKLGDARSLLVFTEELHNLYVGQSMDLYWTSNLVCPSMHEYFQMIEHKTGGLFRLFGRLMAVHSTNPVQVDLTDFTNHLGRYFQTRDDYQNLVSAEYTKQKGFCEDFEEGKFSLPMIHLMQTMPDNLVLRNVWTQRRVNGTATHGQKQTILNLMKEAGTLKFTQDSLGVLYSDVEKSVAELESKFGIENFQLRLIMELLKT | ||||||
Region | 332-356 | Disordered | ||||
Sequence: KNGVPKDPASGSTNGTSNGTSNGTS | ||||||
Compositional bias | 338-356 | Polar residues | ||||
Sequence: DPASGSTNGTSNGTSNGTS | ||||||
Motif | 473-477 | DDXXD motif 2 | ||||
Sequence: DDVED |
Domain
The characteristic DDXXD motif for binding a trinuclear Mg2+ cluster is conserved in both the N-terminal terpene cyclase and C-terminal prenyl transferase domains.
The Mg2+-binding NSE motif in the terpene cyclase domain is not completely conserved, since the asparagine residue in the is substituted with histidine.
Sequence similarities
In the N-terminal section; belongs to the terpene synthase family.
In the C-terminal section; belongs to the FPP/GGPP synthase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length714
- Mass (Da)80,706
- Last updated2016-01-20 v1
- ChecksumDA520A976523611F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 338-356 | Polar residues | ||||
Sequence: DPASGSTNGTSNGTSNGTS |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LC073704 EMBL· GenBank· DDBJ | BAT32889.1 EMBL· GenBank· DDBJ | Genomic DNA |