K7MJC5 · K7MJC5_SOYBN
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta
- GenePFP-BETA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids575 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis.
Catalytic activity
- beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + phosphate + H+
Cofactor
Activity regulation
Allosterically activated by fructose 2,6-bisphosphate.
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 | 106 | diphosphate (UniProtKB | ChEBI) | |||
Binding site | 207 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Site | 208 | Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP | |||
Site | 234 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | |||
Binding site | 235-237 | substrate | |||
Active site | 237 | Proton acceptor | |||
Binding site | 274-275 | substrate; ligand shared between dimeric partners | |||
Binding site | 282-284 | substrate | |||
Binding site | 343 | substrate | |||
Binding site | 448-451 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | ATP binding | |
Molecular Function | diphosphate-fructose-6-phosphate 1-phosphotransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | photosynthesis | |
Biological Process | response to glucose |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta
- EC number
- Short namesPFP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Glycine > Glycine subgen. Soja
Accessions
- Primary accessionK7MJC5
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Proteomic databases
Interaction
Subunit
Tetramer of two alpha (regulatory) and two beta (catalytic) chains.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 98-473 | Phosphofructokinase | |||
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length575
- Mass (Da)63,117
- Last updated2013-01-09 v1
- Checksum51F5FE60D14CB107
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM000850 EMBL· GenBank· DDBJ | KRH02012.1 EMBL· GenBank· DDBJ | Genomic DNA |