P0A796 · PFKA_ECOLI
- ProteinATP-dependent 6-phosphofructokinase isozyme 1
- GenepfkA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids320 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (PubMed:2953977, PubMed:3158524).
In addition, is involved in the utilization of D-sedoheptulose 7-phosphate, an intermediate of the pentose phosphate pathway, via the sedoheptulose bisphosphate bypass pathway (PubMed:19756045).
Catalyzes the phosphorylation of D-sedoheptulose 7-phosphate to D-sedoheptulose 1,7-bisphosphate (PubMed:19756045).
In addition, is involved in the utilization of D-sedoheptulose 7-phosphate, an intermediate of the pentose phosphate pathway, via the sedoheptulose bisphosphate bypass pathway (PubMed:19756045).
Catalyzes the phosphorylation of D-sedoheptulose 7-phosphate to D-sedoheptulose 1,7-bisphosphate (PubMed:19756045).
Catalytic activity
- ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H+
- ATP + D-sedoheptulose 7-phosphate = ADP + D-sedoheptulose 1,7-bisphosphate + H+This reaction proceeds in the forward direction.
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 | 12 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 22-26 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: RGVVR | ||||||
Binding site | 55-60 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: RYSVSD | ||||||
Binding site | 73-74 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RF | ||||||
Binding site | 103-106 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 104 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 126-128 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 128 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 155 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 163 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 170-172 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 186-188 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: GCE | ||||||
Binding site | 212 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 214-216 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: KKH | ||||||
Binding site | 223 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 244 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 250-253 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HIQR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 6-phosphofructokinase complex | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | fructose-6-phosphate binding | |
Molecular Function | GDP binding | |
Molecular Function | identical protein binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | monosaccharide binding | |
Molecular Function | ribonucleotide binding | |
Biological Process | canonical glycolysis | |
Biological Process | fructose 1,6-bisphosphate metabolic process | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | glucose catabolic process | |
Biological Process | glycolytic process | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent 6-phosphofructokinase isozyme 1
- EC number
- Short namesATP-PFK 1 ; Phosphofructokinase 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A796
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 128 | 18000-fold reduction of catalytic rate. | ||||
Sequence: D → S | ||||||
Mutagenesis | 172 | 3.4-fold reduction in turnover numbers. | ||||
Sequence: R → S |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000111950 | 1-320 | ATP-dependent 6-phosphofructokinase isozyme 1 | |||
Sequence: MIKKIGVLTSGGDAPGMNAAIRGVVRSALTEGLEVMGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFRDENIRAVAIENLKKRGIDALVVIGGDGSYMGAMRLTEMGFPCIGLPGTIDNDIKGTDYTIGFFTALSTVVEAIDRLRDTSSSHQRISVVEVMGRYCGDLTLAAAIAGGCEFVVVPEVEFSREDLVNEIKAGIAKGKKHAIVAITEHMCDVDELAHFIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIDLLLAGYGGRCVGIQNEQLVHHDIIDAIENMKRPFKGDWLDCAKKLY |
Proteomic databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P0A796 | moeA P12281 | 2 | EBI-554405, EBI-554393 | |
BINARY | P0A796 | prfC P0A7I4 | 2 | EBI-554405, EBI-556252 | |
BINARY | P0A796 | ucpA P37440 | 2 | EBI-554405, EBI-559387 |
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length320
- Mass (Da)34,842
- Last updated2005-06-07 v1
- ChecksumD03D79F6A5536A41
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 74 | in Ref. 1; CAA26356 | ||||
Sequence: F → C | ||||||
Sequence conflict | 103-104 | in Ref. 1; CAA26356 | ||||
Sequence: GD → DG | ||||||
Sequence conflict | 163 | in Ref. 1; CAA26356 | ||||
Sequence: R → P | ||||||
Sequence conflict | 317-319 | in Ref. 1; CAA26356 | ||||
Sequence: KKL → EKM |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X02519 EMBL· GenBank· DDBJ | CAA26356.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L19201 EMBL· GenBank· DDBJ | AAB03048.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC76898.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77394.1 EMBL· GenBank· DDBJ | Genomic DNA |