HAMAP rule MF_01977
General rule information
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| Accession | MF_01977 |
| Dates | 16-MAY-2014 (Created)
3-SEP-2024 (Last updated, Version 12) |
| Name | Phosphofructokinase_II_P |
| Scope(s) |
Bacteria Eukaryota |
| Template(s) | P29495 (PFP_PROFC); G4STG9 (PFP_META2); Q3KSV5 (PFP_METMH); Q9NGP6 (PFP_MASBA); [ Recover all ] |
| Triggered by |
HAMAP; MF_01977 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | PFP |
| Protein name | RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase; EC=2.7.1.90; AltName: Full=6-phosphofructokinase, pyrophosphate dependent; AltName: Full=PPi-dependent phosphofructokinase; Short=PPi-PFK; AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase; |
| case <OC:Bacteria> | |
| Gene name | Name=pfp; |
| end case | |
Comments
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| FUNCTION | 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. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. |
| CATALYTIC ACTIVITY | Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + phosphate + H(+); Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; |
| ACTIVITY REGULATION | Non-allosteric. |
| PATHWAY | Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- phosphate and glycerone phosphate from D-glucose: step 3/4. |
| SUBUNIT | Homodimer or homotetramer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'P' sub-subfamily. |
Keywords
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Gene Ontology
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| GO:0003872; Molecular function:6-phosphofructokinase activity |
| GO:0006096; Biological process:glycolytic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF00365; PFK; 1; |
| PIRSF | PIRSF036484; PPi-PFK_SMc01852; 1; |
| PRINTS | PR00476; PHFRCTKINASE; 1; |
Features
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| From: PFP_PROFC (P29495) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| SITE | 122 | 122 | /note="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" | D | ||||||||
| BINDING | 149 | 151 | /ligand="substrate" | T-x-D | ||||||||
| BINDING | 194 | 196 | /ligand="substrate" | M-G-R | ||||||||
| BINDING | 323 | 326 | /ligand="substrate" | [HY]-x(2)-R | ||||||||
| ACT_SITE | 151 | 151 | /note="Proton acceptor" | D | ||||||||
| BINDING | 121 | 121 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="catalytic" |
[DE] | ||||||||
| BINDING | 266 | 266 | /ligand="substrate" | E | ||||||||
| BINDING | 12 | 12 | /ligand="diphosphate" /ligand_id="ChEBI:CHEBI:33019" |
G | ||||||||
| SITE | 148 | 148 | /note="Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi" | K | ||||||||
Additional information
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| Size range | 400-436 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | Classification of type A phosphofructokinases into subfamilies was done according to Mueller at al.(2001) (PubMed:11673446) and Bapteste et al.(2003) (PubMed:14585511). |