A0A176VE92 · A0A176VE92_MARPO
- ProteinATP-dependent 6-phosphofructokinase
- GenePFK
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids554 (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
- beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + 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 | 202 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 266-267 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RG | ||||||
Binding site | 291-294 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GNGT | ||||||
Binding site | 292 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Site | 293 | Important for substrate specificity; cannot use PPi as phosphoryl donor | ||||
Sequence: G | ||||||
Binding site | 320-322 | substrate | ||||
Sequence: TID | ||||||
Active site | 322 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 365-367 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 421 | substrate | ||||
Sequence: E | ||||||
Binding site | 473-476 | substrate | ||||
Sequence: YMIR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
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
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Marchantiophyta > Marchantiopsida > Marchantiidae > Marchantiales > Marchantiaceae > Marchantia
Accessions
- Primary accessionA0A176VE92
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 52-85 | Disordered | ||||
Sequence: RLRGDSRRSRRTNRNLTAIRSQDGKAGLESQDDF | ||||||
Domain | 195-497 | Phosphofructokinase | ||||
Sequence: AAIVTCGGLCPGLNDVIRQIVLTLDVYGVKRMLGITYGYRGFFEESLEPIVLTRHLVQNIHLAGGSLLGVSRGGAKTSDIVDTLQEKGINMLFVLGGNGTHAGANAIHEEARRRRMKLAVVGVPKTIDNDILLMDKTFGFDTAVEEAQRAINTAYIEANSAYNGIGIVKLMGRQSGFIAMHASLASGQVDVCLIPEVPFALDGGHGVLQHIQHLIEERGKAVICVAEGAGQDLLPTNNGTDPSGNPILGDIGTHLQREIKKYFKAASITVDIKYIDPTYMIRACRANASDGILCAVLGQNAVH |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length554
- Mass (Da)60,611
- Last updated2016-09-07 v1
- Checksum53A419448BF463D9
Keywords
- Technical term