A0A1C5MCM8 · A0A1C5MCM8_9CLOT
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase
- Genepfp_1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids411 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Catalytic activity
- beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + phosphate + H+
Cofactor
Activity regulation
Non-allosteric.
Pathway
Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12 | diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 113 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Site | 114 | Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP | ||||
Sequence: D | ||||||
Site | 140 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | ||||
Sequence: K | ||||||
Binding site | 141-143 | substrate | ||||
Sequence: TID | ||||||
Active site | 143 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 189-191 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 246 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | diphosphate-fructose-6-phosphate 1-phosphotransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | fructose 6-phosphate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyrophosphate--fructose 6-phosphate 1-phosphotransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium > environmental samples
Accessions
- Primary accessionA0A1C5MCM8
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-326 | Phosphofructokinase | ||||
Sequence: NIIVGQSGGPTAAINSSLAGVYRTAIDRGAKKVYGMRHGIQGLLNEDYIDLSEHIQTDLDVELLKRTPAAYLGSCRYKLPEIHEDIATYDKIFSILDKLEIECFIYIGGNDSMDTIKKLSDYAILRGHPTKFLGVPKTIDNDLALTDHTPGYGSAAKYIGTSVKEIIQDSQALIYDKGLVTIVEIMGRNAGWLVGAAALSKGEDCDGPDLIYVPELPFDIDNFLVRIKELLAEKTFVVVAVSEGIRLADGRYVCELTDGVDFVDAFGHKQLTGTANYLARRLAQEIGCKTRTIELSSMQRAASHLASRIDILEAFQVGGAAVK |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length411
- Mass (Da)45,242
- Last updated2016-11-02 v1
- ChecksumED81793CB68E8DC6