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Annotation rule MF_03185
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General rule information [?]

Accession MF_03185
Dates 16-MAY-2014 (Created)
20-NOV-2019 (Last updated, Version 8)
Name Phosphofructokinase_II_Long_euk
Scope
Eukaryota
Templates C4LZC2 (PFP_ENTHI); P70826 (PFP_BORBU): [Recover all]
case <OC:Eukaryota>
Triggered by
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

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
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
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 [?]

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 RHEA:13613: beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate
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 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
case <OC:Viridiplantae>
Activity regulation Allosterically activated by fructose 2,6-bisphosphate.
end case
case <FT:1> or <FT:2>
Cofactor Mg(2+)
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 [?]

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 [?]

Pfam PF00365; PFK; 1;
PIRSF PIRSF005677; PPi_PFK_PfpB; 1;
PRINTS PR00476; PHFRCTKINASE; 1;
TIGRFAMs TIGR02477; PFKA_PPi; 1;

Features [?]

From: PFP_ENTHI (C4LZC2)
Key     From     To       Description   Tag   Condition   FTGroup
SITE (Optional)     175     175       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 (Optional)     175     175       Important for substrate specificity; cannot use PPi as phosphoryl donor     G  
case <FT:1>
BINDING     80     80       Diphosphate; via amide nitrogen     G  
SITE     201     201       Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi     K  
else case <FT:2>
NP_BIND     144     145       ATP     [RK]-x  
NP_BIND     173     176       ATP     G-[DE]-G-[ST]  
BINDING     80     80       ATP; via amide nitrogen     G  
end case
case <FT:1> or <FT:2>
REGION     202     204       Substrate binding     T-x-D  
REGION (Optional)     241     242       Substrate binding; shared with dimeric partner     K-Y  
REGION     249     251       Substrate binding     M-G-[RH]  
REGION     420     423       Substrate binding     [HY]-x(2)-R  
ACT_SITE     204     204       Proton acceptor     D  
METAL     174     174       Magnesium; catalytic     [DE]  
BINDING     310     310       Substrate     E  
end case

Additional information [?]

Size range 544-1426 amino acids
Related rules MF_01980 (PFP)
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-175 (PFP_ENTHI 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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