HAMAP rule MF_03185
General rule information
[?]
Accession | MF_03185 |
Dates | 16-MAY-2014 (Created)
1-JUN-2023 (Last updated, Version 13) |
Name | Phosphofructokinase_II_Long_euk |
Scope(s) |
Eukaryota |
Template(s) | C4LZC2 (PFP_ENTH1); P70826 (PFP_BORBU); [ Recover all ] |
Triggered by |
case c? <OC:Eukaryota>
HAMAP; MF_01980 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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case <OC:Viridiplantae> and not (<FT:1> or <FT:2>) | |
Identifier | PFPA |
Protein name | RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha; Short=PFP; AltName: Full=6-phosphofructokinase, pyrophosphate dependent; AltName: Full=PPi-PFK; AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase; |
Gene name | Name=PFP-ALPHA; |
else case (<OC:Viridiplantae>) and <FT:1> | |
Identifier | PFPB |
Protein name | RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta; Short=PFP; EC=2.7.1.90; AltName: Full=6-phosphofructokinase, pyrophosphate dependent; AltName: Full=PPi-PFK; AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase; |
Gene name | Name=PFP-BETA; |
else 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; |
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; |
else | |
Identifier | PFKA |
Protein name | RecName: Full=6-phosphofructokinase; EC=2.7.1.-; |
end case |
Comments
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case <OC:Viridiplantae> and not (<FT:1> or <FT:2>) | |
FUNCTION | Regulatory subunit of pyrophosphate--fructose 6-phosphate 1- phosphotransferase. |
else case <OC:Viridiplantae> and <FT:1> | |
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 | Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; |
else 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 | Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; 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 | Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6- bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; 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 | |
case <OC:Viridiplantae> | |
ACTIVITY REGULATION | Allosterically activated by fructose 2,6- bisphosphate. |
end case | |
case <FT:1> or <FT:2> | |
COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; |
end case | |
PATHWAY | Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- phosphate and glycerone phosphate from D-glucose: step 3/4. |
case (<OC:Viridiplantae> or <OC:Apicomplexa>) | |
SUBUNIT | Tetramer of two alpha (regulatory) and two beta (catalytic) chains. |
else | |
SUBUNIT | Homodimer or monomer. |
end case | |
SUBCELLULAR LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily. |
Keywords
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case <OC:Viridiplantae> | |
Allosteric enzyme | |
end case | |
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
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Pfam | PF00365; PFK; 1; |
PIRSF | PIRSF005677; PPi_PFK_PfpB; 1; |
PRINTS | PR00476; PHFRCTKINASE; 1; |
NCBIfam | TIGR02477; PFKA_PPi; 1; |
Features
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From: PFP_ENTH1 (C4LZC2) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
SITE | 175 | 175 | /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" | [DN] | ||||||||
SITE | 175 | 175 | /note="Important for substrate specificity; cannot use PPi as phosphoryl donor" | G | ||||||||
case <FT:1> | ||||||||||||
BINDING | 80 | 80 | /ligand="diphosphate" /ligand_id="ChEBI:CHEBI:33019" |
G | ||||||||
SITE | 201 | 201 | /note="Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi" | K | ||||||||
else case <FT:2> | ||||||||||||
BINDING | 144 | 145 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[RK]-x | ||||||||
BINDING | 173 | 176 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G-[DE]-G-[ST] | ||||||||
BINDING | 80 | 80 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G | ||||||||
end case | ||||||||||||
case <FT:1> or <FT:2> | ||||||||||||
BINDING | 202 | 204 | /ligand="substrate" | T-x-D | ||||||||
BINDING | 241 | 242 | /ligand="substrate" /ligand_note="ligand shared between dimeric partners" |
K-Y | ||||||||
BINDING | 249 | 251 | /ligand="substrate" | M-G-[RH] | ||||||||
BINDING | 420 | 423 | /ligand="substrate" | [HY]-x(2)-R | ||||||||
ACT_SITE | 204 | 204 | /note="Proton acceptor" | D | ||||||||
BINDING | 174 | 174 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="catalytic" |
[DE] | ||||||||
BINDING | 310 | 310 | /ligand="substrate" | E | ||||||||
end case |
Additional information
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Size range | 544-1426 amino acids |
Related rules |
MF_01980 |
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). Phosphoryl donor specificity (ATP or PPi) seems to be determined by a single residue, Asp or Gly-175 (PFP_ENTH1 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. |