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HAMAP rule MF_01979

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General rule information [?]

Accession MF_01979
Dates 16-MAY-2014 (Created)
19-NOV-2022 (Last updated, Version 11)
Name Phosphofructokinase_II_Short
Scope
Bacteria
Eukaryota
Templates Q9WYC5 (PFP_THEMA); Q27705 (PFP_NAEFO); A2E9H3 (PFP2_TRIV3): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

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
pfp
end case

Comments [?]

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 RHEA:13613: beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate
EC 2.7.1.90
Activity regulation Non-allosteric.
Cofactor Mg(2+)
Pathway Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
case <OC:Bacteria>
Subunit Homodimer.
else case <OC:Eukaryota>
Subunit Homotetramer.
end case
Subcellular location Cytoplasm.
Similarity Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily.

Keywords [?]

Cytoplasm
Kinase
Transferase
Glycolysis
Magnesium
Metal-binding

Gene Ontology [?]

GO:0003872; Molecular function: 6-phosphofructokinase activity.
GO:0006096; Biological process: glycolytic process.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF00365; PFK; 1;
PIRSF PIRSF036482; PPi_PFK_TM0289; 1;
PRINTS PR00476; PHFRCTKINASE; 1;

Features [?]

From: PFP_THEMA (Q9WYC5)
Key     From     To       Description   Tag   Condition   FTGroup
SITE     108     108       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     132     134       /ligand="substrate     T-x-D  
BINDING     178     180       /ligand="substrate     M-G-R  
BINDING     300     303       /ligand="substrate     Y-x(2)-R  
ACT_SITE     134     134       Proton acceptor     D  
BINDING     107     107       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="catalytic     D  
BINDING     238     238       /ligand="substrate     E  
BINDING     12     12       /ligand="diphosphate" /ligand_id="ChEBI:CHEBI:33019     G  
SITE     131     131       Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi     K  

Additional information [?]

Size range 411-476 amino acids
Related rules None
Fusion 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).


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