A0A2Z6AQX6 · PVPS_TALVE
- ProteinPreasperterpenoid A synthase PvPS
- GenePvPS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids778 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Bifunctional sesterterpene synthase that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into preasperterpenoid A.
Catalytic activity
- (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphateThis reaction proceeds in the forward direction.
- (2E,6E,10E,14E)-geranylfarnesyl diphosphate = diphosphate + preasperterpenoid AThis reaction proceeds in the forward direction.
Cofactor
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 176 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 176 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 176 | substrate | ||||
Sequence: D | ||||||
Binding site | 180 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 180 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 266-269 | substrate | ||||
Sequence: RVIN | ||||||
Binding site | 310 | substrate | ||||
Sequence: N | ||||||
Binding site | 314-318 | substrate | ||||
Sequence: SWEKE | ||||||
Binding site | 406-407 | substrate | ||||
Sequence: RY | ||||||
Binding site | 499 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 502 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 531 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 538 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 538 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 542 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 542 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 547 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 548 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 625 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 626 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 662 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 669 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 679 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 689 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K |
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 namePreasperterpenoid A synthase PvPS
- Alternative names
Including 3 domains:
- Recommended namePreasperterpenoid A cyclase
- EC number
- Recommended nameGeranylgeranyl diphosphate synthase
- EC number
- Short namesGGDP synthase ; GGS
- Recommended nameGeranylfarnesyl diphosphate synthase
- EC number
- Short namesGFDP synthase
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Trichocomaceae > Talaromyces > Talaromyces sect. Talaromyces
Accessions
- Primary accessionA0A2Z6AQX6
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000453791 | 1-778 | Preasperterpenoid A synthase PvPS | |||
Sequence: MAATKKSTATAAHQIIPSQPTSMSADKFLFSCLQVFVLFFEWARSFLLSTQSRLSAVPAENARLEPSKPISEEEESVIEKPASSITPRYSNLVDPSTYNDLGLCSALPLRVHKFAHLADKGALRAQEDWKRLVGPIRNFTGCLSPRFNGIAVAVPECIPERLEIVTYANEFAFLHDDILDNVGKEEGDHENNEMAAGFGSVLNPADNVKMSASGKSQMQAKLILELLAINEPQAMVLLKCWEGLVKGESGSQHFNFQRLDEYLPHRVINLGQTFWFGIITFAMGLTISPDEAEKANNITDPAYATLALANDYFSWEKEYIEFKQNPTSDDMANAIWIIMKEHSVDLEEAKKICQDKIRESCEEYVRRHRQFEREATGKVSTDLLRYLAALEFSISGNVVWSQYTHRYNFHKPAAKENEDTDDEGAKSDDSKTTLNDSTDSTVVDVKTPATSGLLSSANDVLMSRTAKSLVGPILDVQLPELPDKVVLSPSQYVKSLPSKKVRHHAIDALNIWFNVPEAELEVIKEAIDLLHNSSLMLDDIEDDSPLRRGFPSTHVVYGISQTINSANYLYVMALEMTQRLNSPACLNVFIDELKRLHIGQSLDLYWTANVQCPSLEEYLKMVDYKTGGLFQMVAKLMALKSPMAGRVPDLSNMTTLFGRYFQIRDDYQNLMSEEYTNQKGWCEDLDEGKFSLPLIHSLTTKPNVRLQAMLHQRLINGKMTFEMKKLALDHLAETKSLEYTKEMLGYMYTQLQKEVDFLERQTGSENFLLRLLLKRLQV |
Interaction
Subunit
Hexamer.
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-414 | Terpene cyclase | ||||
Sequence: MAATKKSTATAAHQIIPSQPTSMSADKFLFSCLQVFVLFFEWARSFLLSTQSRLSAVPAENARLEPSKPISEEEESVIEKPASSITPRYSNLVDPSTYNDLGLCSALPLRVHKFAHLADKGALRAQEDWKRLVGPIRNFTGCLSPRFNGIAVAVPECIPERLEIVTYANEFAFLHDDILDNVGKEEGDHENNEMAAGFGSVLNPADNVKMSASGKSQMQAKLILELLAINEPQAMVLLKCWEGLVKGESGSQHFNFQRLDEYLPHRVINLGQTFWFGIITFAMGLTISPDEAEKANNITDPAYATLALANDYFSWEKEYIEFKQNPTSDDMANAIWIIMKEHSVDLEEAKKICQDKIRESCEEYVRRHRQFEREATGKVSTDLLRYLAALEFSISGNVVWSQYTHRYNFHKPAA | ||||||
Motif | 176-180 | DDXXD 1 | ||||
Sequence: DDILD | ||||||
Motif | 310-318 | NSE/DTE | ||||
Sequence: NDYFSWEKE | ||||||
Compositional bias | 414-433 | Basic and acidic residues | ||||
Sequence: AKENEDTDDEGAKSDDSKTT | ||||||
Region | 415-778 | Prenyltransferase | ||||
Sequence: KENEDTDDEGAKSDDSKTTLNDSTDSTVVDVKTPATSGLLSSANDVLMSRTAKSLVGPILDVQLPELPDKVVLSPSQYVKSLPSKKVRHHAIDALNIWFNVPEAELEVIKEAIDLLHNSSLMLDDIEDDSPLRRGFPSTHVVYGISQTINSANYLYVMALEMTQRLNSPACLNVFIDELKRLHIGQSLDLYWTANVQCPSLEEYLKMVDYKTGGLFQMVAKLMALKSPMAGRVPDLSNMTTLFGRYFQIRDDYQNLMSEEYTNQKGWCEDLDEGKFSLPLIHSLTTKPNVRLQAMLHQRLINGKMTFEMKKLALDHLAETKSLEYTKEMLGYMYTQLQKEVDFLERQTGSENFLLRLLLKRLQV | ||||||
Region | 416-454 | Disordered | ||||
Sequence: ENEDTDDEGAKSDDSKTTLNDSTDSTVVDVKTPATSGLL | ||||||
Motif | 538-542 | DDXXD 2 | ||||
Sequence: DDIED |
Domain
The conserved DDXXD motifs as well as the NSE/DTE motif are important for the catalytic activity, presumably through binding to Mg2+.
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
- Length778
- Mass (Da)87,884
- Last updated2018-10-10 v1
- Checksum0485E61AB9C5DC71
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 414-433 | Basic and acidic residues | ||||
Sequence: AKENEDTDDEGAKSDDSKTT |