A0A0J2D5M9 · A0A0J2D5M9_ECOLX
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids320 (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
- beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + 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 | 12 | ATP (UniProtKB | ChEBI) | |||
Binding site | 22-26 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 55-60 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 73-74 | ATP (UniProtKB | ChEBI) | |||
Binding site | 103-106 | ATP (UniProtKB | ChEBI) | |||
Binding site | 104 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 126-128 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 128 | Proton acceptor | |||
Binding site | 155 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 163 | substrate; ligand shared between dimeric partners | |||
Binding site | 170-172 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 186-188 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 212 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 214-216 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 223 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 244 | substrate; ligand shared between dimeric partners | |||
Binding site | 250-253 | substrate; ligand shared between dimeric partners; in other chain | |||
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A0J2D5M9
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-276 | Phosphofructokinase | |||
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)34,856
- Last updated2015-10-14 v1
- MD5 Checksum1849437F91007D95834BAE7EEE5E902B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AASATZ010000016 EMBL· GenBank· DDBJ | EFA4418829.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AASKVF010000009 EMBL· GenBank· DDBJ | EFD6884283.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AASWBF010000011 EMBL· GenBank· DDBJ | EFH4960772.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AATCLQ010000011 EMBL· GenBank· DDBJ | EFJ6481763.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AATLZG010000012 EMBL· GenBank· DDBJ | EFM8154528.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAXDPX010000013 EMBL· GenBank· DDBJ | EGO6679584.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DABDSA010000015 EMBL· GenBank· DDBJ | HAI2142445.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
VZEL01000014 EMBL· GenBank· DDBJ | KAB0123776.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAWPMK010000001 EMBL· GenBank· DDBJ | MDW9351271.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
VLTB01000389 EMBL· GenBank· DDBJ | NDR94286.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LRKC01000161 EMBL· GenBank· DDBJ | OKV06213.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
PPHQ01000012 EMBL· GenBank· DDBJ | PNY66853.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UGBW01000003 EMBL· GenBank· DDBJ | STH84840.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UGEE01000003 EMBL· GenBank· DDBJ | STK92730.1 EMBL· GenBank· DDBJ | Genomic DNA |