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Annotation rule MF_01976
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General rule information [?]

Accession MF_01976
Dates 16-MAY-2014 (Created)
19-NOV-2019 (Last updated, Version 8)
Name Phosphofructokinase_III
Scope
Archaea
Bacteria
Templates Q59126 (PFP_AMYME); Q9L1L8 (PFKA2_STRCO): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

case <FTTag:PPI>
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 <FTTag:ATP>
Identifier
PFKA
Protein name
RecName: Full=ATP-dependent 6-phosphofructokinase;
Short=ATP-PFK;
Short=Phosphofructokinase;
EC 2.7.1.11;
AltName: Full=Phosphohexokinase;
Gene name
pfkA
else
Identifier
PFP
Protein name
RecName: Full=6-phosphofructokinase;
EC 2.7.1.-;
end case

Comments [?]

case <FTTag:PPI>
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 <FTTag:ATP>
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 or homotetramer.
Subcellular location Cytoplasm.
Similarity Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.

Keywords [?]

case <FTTag:ATP>
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 PIRSF000532; ATP_PFK_prok; 1;
PRINTS PR00476; PHFRCTKINASE; 1;
TIGRFAMs TIGR02483; PFK_mixed; 1;
PROSITE PS00433; PHOSPHOFRUCTOKINASE; 1;

Features [?]

From: PFP_AMYME (Q59126)
Key     From     To       Description   Tag   Condition   FTGroup
SITE (Optional)     104     104       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   PPI   D  
SITE (Optional)     104     104       Important for substrate specificity; cannot use PPi as phosphoryl donor   ATP   G  
REGION     125     127       Substrate binding     T-x-D  
REGION     169     171       Substrate binding     M-G-[RH]  
REGION     271     274       Substrate binding     [HY]-x(2)-R  
ACT_SITE     127     127       Proton acceptor     D  
METAL     103     103       Magnesium; catalytic     [DEN]  
BINDING (Optional)     162     162       Substrate; shared with dimeric partner     R  
BINDING     221     221       Substrate     E  
BINDING (Optional)     265     265       Substrate; shared with dimeric partner     [RK]  
case <FTTag:PPI>
BINDING     10     10       Diphosphate; via amide nitrogen     G  
SITE     124     124       Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi     K  
end case
case <FTTag:ATP>
From: PFKA2_STRCO (Q9L1L8)
NP_BIND     72     73       ATP     [RK]-x  
NP_BIND     102     105       ATP     G-[DEN]-G-[ST]  
BINDING     10     10       ATP; via amide nitrogen     G  
end case

Additional information [?]

Size range 336-384 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). Phosphoryl donor specificity (ATP or PPi) seems to be determined by a single residue, Asp or Gly-104 (PFP_AMYME 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.