A0A6N7S5N2 · A0A6N7S5N2_9FIRM
- 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
- 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 | 12 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 22-26 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: RAVTR | ||||||
Binding site | 73-74 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RL | ||||||
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: MGN | ||||||
Binding site | 186-188 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: GAE | ||||||
Binding site | 215-217 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: KRH | ||||||
Binding site | 224 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 245 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 251-254 | 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 | 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 > Erysipelotrichia > Erysipelotrichales > Erysipelotrichaceae > Holdemania
Accessions
- Primary accessionA0A6N7S5N2
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-277 | Phosphofructokinase | ||||
Sequence: RIGILTSGGDAPGMNAAIRAVTRVALANGFEVMGIKDGYRGLVEGNYIPMDKSTVSDILNRGGTVLGSARLTEFKDLEIQKKAVQTLQNAKIDAIVVIGGDGSYRGAMALTKLGINCIGLPGTIDNDIPGTDFTIGFDTALNTVVEAVDKLRDTSSSHHRCSVVEVMGNRCGDLAVWAAISCGAEIVITPETGYDELDVLERLRYLDKAVKKRHAIVVISEKIADVDELARKISQNTGFAGRATVLGHVQRGGSPSPRDRVLASMMGEKAVDLL |
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)34,338
- Last updated2020-10-07 v1
- Checksum5D15DC8CD37DD255
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
WKPJ01000009 EMBL· GenBank· DDBJ | MSA89174.1 EMBL· GenBank· DDBJ | Genomic DNA |