A0A858E7G0 · GGDPS_MELLP
- ProteinGeranylgeranyl pyrophosphate synthase
- GeneGGDPS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids364 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Geranylgeranyl pyrophosphate synthase that catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate (PubMed:32913319).
Does not show any monoterpene nor sesquiterpene synthase activity (PubMed:32913319).
Does not show any monoterpene nor sesquiterpene synthase activity (PubMed:32913319).
Catalytic activity
- dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 Mg2+ ions per subunit.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 77 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 80 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 109 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 116 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 116 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 120 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 120 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 125 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 126 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 148 | Important for determining product chain length | ||||
Sequence: Y | ||||||
Binding site | 210 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 211 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 246 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 249 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 253 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 262 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 272 | 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 | isoprenoid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGeranylgeranyl pyrophosphate synthase
- EC number
- Short namesGGPP synthase ; GGPPSase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Pucciniomycotina > Pucciniomycetes > Pucciniales > Melampsoraceae > Melampsora
Accessions
- Primary accessionA0A858E7G0
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000457150 | 1-364 | Geranylgeranyl pyrophosphate synthase | |||
Sequence: MKPVPSTNGKVDDKVEHHNLSSSSSSSSSSSSSDTKFNISNRYGNFLQRLEALDIWPESNEQILLEPYTYLTNIPGKEIRSMMIDAFNHWLQVPRPALEIIKKIVGQLHTASLLMDDVEDDSDLRRGVPVTHKIYGIPQTINTANYVYFLAYQELTKLKPCLRSDATTDLWSLVNDELLQLHRGQGMDLYWRDSLTCPTEEEYLQMVNNKTGGLFRIAIKLMIALSPIPETPDYLPLVNLVGIIFQIRDDLLNLSSVYTKNKGFCEDLTEGKFSFPIVHSIRSDSTNHQLMNILRQKPTDIGTKAFAVSYMKDRTKSLEYTRGVLICLEEQAIEEVTRLGGNPALESIFELMHVLPSPPATDQN |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-34 | Disordered | ||||
Sequence: MKPVPSTNGKVDDKVEHHNLSSSSSSSSSSSSSD | ||||||
Compositional bias | 20-34 | Polar residues | ||||
Sequence: LSSSSSSSSSSSSSD | ||||||
Motif | 116-120 | DDXXD 2 | ||||
Sequence: DDVED |
Sequence similarities
Belongs to the FPP/GGPP synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length364
- Mass (Da)41,198
- Last updated2021-09-29 v1
- Checksum172BE22D341F3076
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 20-34 | Polar residues | ||||
Sequence: LSSSSSSSSSSSSSD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL883097 EMBL· GenBank· DDBJ | EGG09623.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
MK946437 EMBL· GenBank· DDBJ | QIG55789.1 EMBL· GenBank· DDBJ | mRNA |