Q8ZWV0 · PGMI_PYRAE
- ProteinBifunctional phosphoglucose/phosphomannose isomerase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids302 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.
Miscellaneous
The lack of any movement in response to the binding of ligand may be due to its inherent thermostability, which would tend to restrict any flexibility in the protein.
Catalytic activity
- alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Activity regulation
Inhibited by 5-phosphoarabinonate (PAB) and 6-phosphogluconate.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.7 mM | glucose 6-phosphate | 50 | ||||
0.3 mM | fructose 6-phosphate | 50 | ||||
1.9 mM | glucose 6-phosphate | 80 | ||||
0.06 mM | fructose 6-phosphate | 80 | ||||
0.49 mM | mannose 6-phosphate | 80 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
50 mmol/min/mg | 50 | with glucose 6-phosphate as substrate | |||
31.3 mmol/min/mg | 50 | with fructose 6-phosphate as substrate | |||
150 mmol/min/mg | 80 | with glucose 6-phosphate as substrate | |||
109 mmol/min/mg | 80 | with fructose 6-phosphate as substrate | |||
117 mmol/min/mg | 80 | with mannose 6-phosphate as substrate |
pH Dependence
Optimum pH is 7.4.
Temperature Dependence
Optimum temperature is 100 degrees Celsius.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48 | substrate | ||||
Sequence: S | ||||||
Binding site | 87 | substrate | ||||
Sequence: S | ||||||
Binding site | 92 | substrate | ||||
Sequence: T | ||||||
Active site | 203 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 219 | Proton donor | ||||
Sequence: H | ||||||
Active site | 298 | Proton acceptor | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | carbohydrate derivative binding | |
Molecular Function | glucose-6-phosphate isomerase activity | |
Molecular Function | mannose-6-phosphate isomerase activity | |
Biological Process | carbohydrate derivative metabolic process | |
Biological Process | carbohydrate metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional phosphoglucose/phosphomannose isomerase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Pyrobaculum
Accessions
- Primary accessionQ8ZWV0
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000227794 | 1-302 | Bifunctional phosphoglucose/phosphomannose isomerase | |||
Sequence: MSQLLQDYLNWENYILRRVDFPTSYVVEGEVVRIEAMPRLYISGMGGSGVVADLIRDFSLTWNWEVEVIAVKDYFLKARDGLLIAVSYSGNTIETLYTVEYAKRRRIPAVAITTGGRLAQMGVPTVIVPKASAPRAALPQLLTAALHVVAKVYGIDVKIPEGLEPPNEALIHKLVEEFQKRPTIIAAESMRGVAYRVKNEFNENAKIEPSVEILPEAHHNWIEGSERAVVALTSPHIPKEHQERVKATVEIVGGSIYAVEMHPKGVLSFLRDVGIASVKLAEIRGVNPLATPRIDALKRRLQ |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-160 | SIS | ||||
Sequence: VEGEVVRIEAMPRLYISGMGGSGVVADLIRDFSLTWNWEVEVIAVKDYFLKARDGLLIAVSYSGNTIETLYTVEYAKRRRIPAVAITTGGRLAQMGVPTVIVPKASAPRAALPQLLTAALHVVAKVYGIDVKIP |
Sequence similarities
Belongs to the PGI/PMI family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length302
- Mass (Da)33,548
- Last updated2002-03-01 v1
- Checksum853E7B8E4BA9AA21
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE009441 EMBL· GenBank· DDBJ | AAL63599.1 EMBL· GenBank· DDBJ | Genomic DNA |