A0A1U8QLG8 · PBCB_EMENI
- ProteinGeranylgeranyl pyrophosphate synthase AN1592
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids397 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-814,15-diene (PD) (PubMed:22506079, PubMed:27098256).
Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256).
The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256).
Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-814,15-diene (PubMed:22506079, PubMed:27098256).
The putative roles of the remaining cluster enzymes in ent-pimara-814,15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-814,15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256).
The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256).
Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-814,15-diene (PubMed:22506079, PubMed:27098256).
The putative roles of the remaining cluster enzymes in ent-pimara-814,15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-814,15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Catalytic activity
- dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate
Cofactor
Note: Binds 3 Mg2+ ions per subunit.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 120 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 123 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 152 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 159 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 159 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 163 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 163 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 168 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 169 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 191 | Important for determining product chain length | ||||
Sequence: Y | ||||||
Binding site | 247 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 248 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 281 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 284 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 288 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 298 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 308 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | dimethylallyltranstransferase activity | |
Molecular Function | farnesyltranstransferase activity | |
Molecular Function | geranyltranstransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | prenyltransferase activity | |
Biological Process | alcohol biosynthetic process | |
Biological Process | isoprenoid 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 nameGeranylgeranyl pyrophosphate synthase AN1592
- EC number
- Short namesGGPP synthase ; GGPPSase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionA0A1U8QLG8
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450840 | 1-397 | Geranylgeranyl pyrophosphate synthase AN1592 | |||
Sequence: MSPPLDSALEPLSEYKETAFPRTEKDPSQYKEHDLVTPEKEIQTGYFSPRGSHSSHGSHDSSASSNISLDDARMSDVNNSPNVFHDDPDTIDEKLSMYWKAANETVIREPYDYIAGIPGKEIRRKLLEAFNHWYKVDEQSCQAIATTVGMAHNASLLIDDIQDSSKLRRGVPCAHEVFGIAQTINSANYVYFLAQNQLFRLRSWPQAISVFNEEMVNLHRGQGMELFWRDNLLPPSMDDYLQMIANKTGGLFRMIVRLLQTSSRQVIDVEQLVDVLGLYFQILDDYKNIREEKMAAQKGFFEDLTEGKFSFPICHAIGEGAKNRTALLHMLRLKTDDMKIKQEAVCILDNAGSLDYTREVLYGLDRKARSLLREFKTPNPFMEALLDAMLSSLQACH |
Expression
Induction
Expression is positively regulated by the cluster-specific transcription factor pbcR.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-67 | Disordered | ||||
Sequence: MSPPLDSALEPLSEYKETAFPRTEKDPSQYKEHDLVTPEKEIQTGYFSPRGSHSSHGSHDSSASSNI | ||||||
Compositional bias | 17-39 | Basic and acidic residues | ||||
Sequence: ETAFPRTEKDPSQYKEHDLVTPE | ||||||
Compositional bias | 47-67 | Polar residues | ||||
Sequence: FSPRGSHSSHGSHDSSASSNI |
Sequence similarities
Belongs to the FPP/GGPP synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length397
- Mass (Da)45,185
- Last updated2017-05-10 v1
- Checksum46E5E26D2E851FA6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 17-39 | Basic and acidic residues | ||||
Sequence: ETAFPRTEKDPSQYKEHDLVTPE | ||||||
Compositional bias | 47-67 | Polar residues | ||||
Sequence: FSPRGSHSSHGSHDSSASSNI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AACD01000025 EMBL· GenBank· DDBJ | EAA64299.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BN001307 EMBL· GenBank· DDBJ | CBF85177.1 EMBL· GenBank· DDBJ | Genomic DNA |