A0A2N0UQK4 · A0A2N0UQK4_9FIRM
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA_2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids358 (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 | 11 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 75-76 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RQ | ||||||
Binding site | 112-115 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GNGT | ||||||
Binding site | 113 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Site | 114 | Important for substrate specificity; cannot use PPi as phosphoryl donor | ||||
Sequence: G | ||||||
Binding site | 135-137 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 137 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 172 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 179-181 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGH | ||||||
Binding site | 232 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 276 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 282-285 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HFQR |
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 > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Ruminococcus
Accessions
- Primary accessionA0A2N0UQK4
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer or homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-308 | Phosphofructokinase | ||||
Sequence: RVGILTSGGDCQGLNATIRAVAKTLYNQLGNDVEIIGIIDGYRGLIYGETRKMKPENFSGILTMGGTILGTSRQPFKLMRVVDENSVDKVEAMKKNYKKLGLDCLVVLGGNGTQKTANLLREEGLNVVSLPKTIDNDLWGTDKTFGFQSAVDIATNVIDCIHSTATSHGRVFIIEVMGHKVGWLTLYAGIAGGADIILIPEIPYDIDSVVKTIKSRTAGGKNFSILAVAEGAISKEIAALPKKQRKAAVAEMKYPSISYQIAHDIEEATGQETRVTVPGHFQRGGSPDAYDRVISTRFGVKAAELI |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length358
- Mass (Da)38,586
- Last updated2018-04-25 v1
- ChecksumB7CF23A55E4CB232