A0A1I6DLE1 · A0A1I6DLE1_9FIRM
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids365 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic activity
- ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H+
Cofactor
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 | 16 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 79-80 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RD | ||||||
Binding site | 119-122 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 120 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 121 | Important for substrate specificity; cannot use PPi as phosphoryl donor | ||||
Sequence: G | ||||||
Binding site | 142-144 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 144 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 179 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 186-188 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 239 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 283 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 289-292 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HLQR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 6-phosphofructokinase complex | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | diphosphate-fructose-6-phosphate 1-phosphotransferase activity | |
Molecular Function | fructose-6-phosphate binding | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | monosaccharide binding | |
Biological Process | canonical glycolysis | |
Biological Process | fructose 1,6-bisphosphate metabolic process | |
Biological Process | fructose 6-phosphate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent 6-phosphofructokinase
- EC number
- Short namesATP-PFK ; Phosphofructokinase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Desulfallaceae > Desulfoscipio
Accessions
- Primary accessionA0A1I6DLE1
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-314 | Phosphofructokinase | ||||
Sequence: RIGVLTGGGDAPGLNAVIRAVVKTAIREYGMNVVGFENGFGGLIKNQARELTEFDVIGILPRGGTILGTTNRDNPFHYPVIKGDKKIFADVSDRVFENISIHGIEALVVIGGDGSLAIGKELNDQGLKVVGVPKTIDNDLSATDQTFGFDTALATATEAIDKLHTTAESHHRVMVLELMGRYAGWIALAAGLAGGADVILIPEIPYNIDVVVEKINARSQERKKFSIVVVAEGAKPLGGEMVVSKHVEDSFDPVRLGGVGNVVAQAIESATDKETRVTVLGHLQRGGSPTAYDRILATRYGTGAVNL |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length365
- Mass (Da)38,578
- Last updated2017-11-22 v1
- Checksum265B3744F40BC3E8
Keywords
- Technical term