A0A6G8CII8 · A0A6G8CII8_9BURK
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids350 (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 | 10 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 105-108 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGT | ||||||
Binding site | 106 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 107 | Important for substrate specificity; cannot use PPi as phosphoryl donor | ||||
Sequence: G | ||||||
Binding site | 128-130 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 130 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 165 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 172-174 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 224 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 268 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 274-277 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HLQR |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Diaphorobacter
Accessions
- Primary accessionA0A6G8CII8
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer or homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-299 | Phosphofructokinase | ||||
Sequence: RVGVLTGGGDCPGLNAVIRAVTKSLIGQGQCEVFGIEDGFQGLMEDTPRVQALSWDQVSGILHRGGTILGTSNSANPLRDDATKELVARNAKALGLDVLVVIGGDGTMSLAHGLADVGLQCVGVPKTIDNDIAHCERSFGFDTAVATVTDALHRIESTANSHHRVMIVETMGRHAGWIALESGLAGGADIILLPEIDYDIAAIALRCRERELRQRYTIICIGEGAKESGASLTVRERVEGSPDPVRLGGVAHVLRERLQPHLKSEVRATVLGHLQRGGDPTPFDRVLATRFGHRAAQL |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length350
- Mass (Da)37,318
- Last updated2020-08-12 v1
- ChecksumDE835394E2EF944A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP049910 EMBL· GenBank· DDBJ | QIL78699.1 EMBL· GenBank· DDBJ | Genomic DNA |