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HAMAP rule MF_01980

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General rule information [?]

Accession MF_01980
Dates 16-MAY-2014 (Created)
1-JUN-2023 (Last updated, Version 13)
Name Phosphofructokinase_II_Long
Scope
Bacteria
Templates P70826 (PFP_BORBU); C4LZC2 (PFP_ENTH1): [Recover all]
case <OC:Bacteria>
Triggered by
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

case <FT:1>
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;
Gene name
pfp
else case <FT:2>
Identifier
PFKA
Protein name
RecName: Full=Probable ATP-dependent 6-phosphofructokinase;
Short=ATP-PFK;
Short=Phosphofructokinase;
EC 2.7.1.11;
AltName: Full=Phosphohexokinase;
Gene name
pfkA
else
Identifier
PFKA
Protein name
RecName: Full=6-phosphofructokinase;
EC 2.7.1.-;
Gene name
pfk
end case

Comments [?]

case <FT:1>
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.
else case <FT:2>
Function Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic activity RHEA:16109: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
EC 2.7.1.11
else
Function Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate, the first committing step of glycolysis.
end case
Cofactor Mg(2+)
Pathway Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subunit Homodimer.
Subcellular location Cytoplasm.
Similarity Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.

Keywords [?]

Cytoplasm
Kinase
Transferase
Glycolysis
Magnesium
Metal-binding
case <FT:2>
ATP-binding
Nucleotide-binding
end case

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 PIRSF005677; PPi_PFK_PfpB; 1;
PRINTS PR00476; PHFRCTKINASE; 1;
NCBIfam TIGR02477; PFKA_PPi; 1;

Features [?]

From: PFP_BORBU (P70826)
Key     From     To       Description   Tag   Condition   FTGroup
SITE (Optional)     177     177       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  
SITE (Optional)     177     177       Important for substrate specificity; cannot use PPi as phosphoryl donor     G  
case <FT:1>
BINDING     82     82       /ligand="diphosphate" /ligand_id="ChEBI:CHEBI:33019     G  
SITE     203     203       Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi     K  
else case <FT:2>
BINDING     146     147       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     [RK]-x  
BINDING     175     178       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     G-[DE]-G-[ST]  
BINDING     82     82       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     G  
end case
case <FT:1> or <FT:2>
BINDING     204     206       /ligand="substrate" /ligand_note="ligand shared between dimeric partners" /note="in other chain     T-x-D  
BINDING (Optional)     243     244       /ligand="substrate" /ligand_note="ligand shared between dimeric partners     K-Y  
BINDING     251     253       /ligand="substrate" /ligand_note="ligand shared between dimeric partners" /note="in other chain     M-G-[RH]  
BINDING     428     431       /ligand="substrate" /ligand_note="ligand shared between dimeric partners" /note="in other chain     [HY]-x(2)-R  
ACT_SITE     206     206       Proton acceptor     D  
BINDING     176     176       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="catalytic     [DE]  
BINDING     312     312       /ligand="substrate" /ligand_note="ligand shared between dimeric partners" /note="in other chain     E  
end case

Additional information [?]

Size range 548-573 amino acids
Related rules MF_03185 (PFPA)
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). Phosphoryl donor specificity (ATP or PPi) seems to be determined by a single residue, Asp or Gly-177 (PFP_BORBU numbering) according to Chi et al.(2000) (PubMeed:11001940), Moore et al.(2002) (PubMed:12015149), and Bapteste et al.(2003) (PubMed:14585511) and references therein.


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