A0A7C6PDY7 · A0A7C6PDY7_9FIRM
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids361 (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 | 10 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 72-73 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RD | ||||||
Binding site | 113-116 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGT | ||||||
Binding site | 114 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 115 | Important for substrate specificity; cannot use PPi as phosphoryl donor | ||||
Sequence: G | ||||||
Binding site | 138-140 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 140 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 175 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 182-184 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 235 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 279 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 285-288 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HIQR |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Syntrophomonadaceae
Accessions
- Primary accessionA0A7C6PDY7
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer or homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-310 | Phosphofructokinase | ||||
Sequence: RVGILTGGGDCPGLNAVIRAAAKTLFTGGVEVLGFRDGYRGIIEKDWMPIDKRAISGLLHRGGTILGTNNRDNPFNFPVKTPEGNTEYCDASNQLLANMRELKLDSLISIGGDGTLSIARELVAKDKDTHIVGVPKTIDNDLAATDQTFGFDTAVATATSALDKLHSTAESHHRVMVLEVMGRYAGWIALWSGFAGGADVILIPEIPWSLESIIEKIEDRQKEGKPFSIIVVAEGTPGPDGKQVIRERIEESGDPVRLGGIGQVVGALVEQATGMETRVTVLGHIQRGGSPSPMDRILATRFGVAAAEL |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length361
- Mass (Da)38,413
- Last updated2020-12-02 v1
- Checksum8ACE25A92A65382D