Q6EVA0 · Q6EVA0_BACIU
- ProteinIsopentenyl-diphosphate delta-isomerase
- Geneidi-2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids349 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic activity
- isopentenyl diphosphate = dimethylallyl diphosphate
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 6-7 | substrate | ||||
Sequence: RK | ||||||
Binding site | 62-64 | FMN (UniProtKB | ChEBI) | ||||
Sequence: AMT | ||||||
Binding site | 93 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 122 | FMN (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 152 | substrate | ||||
Sequence: Q | ||||||
Binding site | 153 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 184 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 214 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 258-259 | FMN (UniProtKB | ChEBI) | ||||
Sequence: GG | ||||||
Binding site | 280-281 | FMN (UniProtKB | ChEBI) | ||||
Sequence: AG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | FMN binding | |
Molecular Function | isopentenyl-diphosphate delta-isomerase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | NADPH binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | isoprenoid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIsopentenyl-diphosphate delta-isomerase
- EC number
- Short namesIPP isomerase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionQ6EVA0
Subcellular Location
Interaction
Subunit
Homooctamer. Dimer of tetramers.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 166-324 | FMN-dependent dehydrogenase | ||||
Sequence: ALKRIEQICSRVSVPVIVKEVGFGMSKASAGKLYEAGAAAVDIGGYGGTNFSKIENLRRQRQISFFNSWGISTAASLAEIRSEFPASTMIASGGLQDALDVAKAIALGASCTGMAGHFLKALTDSGEEGLLEEIQLILEELKLIMTVLGARTIADLQKA |
Sequence similarities
Belongs to the IPP isomerase type 2 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length349
- Mass (Da)37,221
- Last updated2005-05-10 v1
- Checksum3EA275B6EDEAB587
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ781076 EMBL· GenBank· DDBJ | CAG77478.1 EMBL· GenBank· DDBJ | Genomic DNA |