A0A922G1V8 · A0A922G1V8_CARIL
- ProteinATP-dependent 6-phosphofructokinase
- GenePFK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids529 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 AMP.
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 | 181 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 245-246 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RG | ||||||
Binding site | 270-273 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GNGT | ||||||
Binding site | 271 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Site | 272 | Important for substrate specificity; cannot use PPi as phosphoryl donor | ||||
Sequence: G | ||||||
Binding site | 299-301 | substrate | ||||
Sequence: TID | ||||||
Active site | 301 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 344-346 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 400 | substrate | ||||
Sequence: E | ||||||
Binding site | 452-455 | substrate | ||||
Sequence: YMIR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding |
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
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fagales > Juglandaceae > Carya
Accessions
- Primary accessionA0A922G1V8
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 174-476 | Phosphofructokinase | ||||
Sequence: AAIVTCGGLCPGLNDVIRQIVITLEIYGVKKIVGIPFGYRGFSDKELTEMPLSRKVVQNVHLSGGSLLGVSRGGPDVSEIVDRMEERGISMLFVLGGNGTHAGAEAIHNECRKRQMRVAVVGVPKTIDNDILLMDKTFGFDTAVEEAQRAINSAYIEAHSAYHGVGIVKLMGRSSGYIAMHASLASGQIDICLIPEVRFNLHGPHGVLQHLKYLIETKGSAVVCVAEGAGQDFLQKTNAKDASGNIVLGDIGVHIQQETKKHFKEIGVPVDVKHIDPTYMIRACRANASDGILCTVLGQNAVH |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length529
- Mass (Da)58,372
- Last updated2023-02-22 v1
- ChecksumFFD1A70EC6261F8C