A0A7V2AZJ9 · A0A7V2AZJ9_RHOMR
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids375 (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 | 14 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 77-78 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RA | ||||||
Binding site | 112-115 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGT | ||||||
Binding site | 113 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 114 | Important for substrate specificity; cannot use PPi as phosphoryl donor | ||||
Sequence: G | ||||||
Binding site | 135-137 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 137 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 172 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 179-181 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 232 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 276 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 282-285 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR |
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 > Rhodothermota > Rhodothermia > Rhodothermales > Rhodothermaceae > Rhodothermus
Accessions
- Primary accessionA0A7V2AZJ9
Subcellular Location
Interaction
Subunit
Homodimer or homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-307 | Phosphofructokinase | ||||
Sequence: RIGLLTGGGDCPGMNAVIRAVTKSLILQANAEVIGFEDGYEGLIEGRFRTLEYGDVSGILTRGGTILGTSNRANPFRYYRRGEADVSAEVVALYRELELDGIVAIGGDGTMTIAHGLSERGLRFVGVPKTIDNDIWGTEHTLGFDTAVHVATEAIDRLHTTAQSHHRVMICETMGRYAGWIALYAGVAAGADVILIPELPFDIEVVAEVCRERESDGRRFTIIVVAEGARPEGGAMHVHTQVPESPDPLRLGGIGYEVERQLRERLRSEVRTTVLGHVQRGGTPTPYDRNLASVFGTYAAAL |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)40,124
- Last updated2021-06-02 v1
- Checksum2CD47BD5CB5124CA