A0A9D1D8J4 · A0A9D1D8J4_9FIRM
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids325 (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
Activity regulation
Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.
Pathway
Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 15 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 25-29 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: RAVVR | ||||||
Binding site | 76-77 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RS | ||||||
Binding site | 106-109 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGT | ||||||
Binding site | 107 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 129-131 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 131 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 158 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 166 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 173-175 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 218-220 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: KTH | ||||||
Binding site | 227 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 248 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 254-257 | 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 | 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 > Oscillospiraceae > Oscillospiraceae incertae sedis > Candidatus Avoscillospira
Accessions
- Primary accessionA0A9D1D8J4
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-280 | Phosphofructokinase | ||||
Sequence: RIGVLTSGGDAPGMNAAIRAVVRGCLYRGIECVGIRRGYNGLINGDILRMDAGTVTHIINRGGTILYTARSDEFRTEEGQLRAAATCKLVGLDGIVAIGGDGTFRGAEALAKTGVSVVGVPATIDNDIACTDYTIGFDTASNTAVDAIDRLRDTMQSHERCSVVEVMGRNAGHLALYVGLAVGATAVLMPELPMDFDRDVVEKIRRARLAGKTHFMIVVAEGAGKAIEIGEQIHEELGLDPRVTILGHIQRGGTPTARDRVMATRMGYTAVEVL |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length325
- Mass (Da)34,433
- Last updated2023-05-03 v1
- ChecksumF060F3ADBDFB8D62