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HAMAP rule MF_01976

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_01976
Accession MF_01976
Dates 16-MAY-2014 (Created)
03-SEP-2024 (Last updated, Version 15)
Name Phosphofructokinase_III
Scope(s) Archaea
Bacteria
Template(s) Q59126; Q9L1L8; [ Recover all ]
Triggered by HAMAP; MF_01976 (Get profile general information and statistics)

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 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 Name=pfkA;
else
Identifier PFP
Protein name RecName: Full=6-phosphofructokinase;
                 EC=2.7.1.-;
end case

Comments [?]

case <FTTag:PPI>
FUNCTIONCatalyzes 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 + phosphate + H(+); 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 REGULATIONNon-allosteric.
else case <FTTag:ATP>
FUNCTIONCatalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
CATALYTIC ACTIVITY Reaction=beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6- bisphosphate + ADP + 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
FUNCTIONCatalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate, the first committing step of glycolysis.
end case
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
PATHWAYCarbohydrate degradation; glycolysis; D-glyceraldehyde 3- phosphate and glycerone phosphate from D-glucose: step 3/4.
SUBUNITHomodimer or homotetramer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.

Keywords [?]

Cytoplasm
Kinase
Transferase
Glycolysis
Magnesium
Metal-binding
case <FTTag:ATP>
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 PIRSF000532; ATP_PFK_prok; 1;
PRINTS PR00476; PHFRCTKINASE; 1;
NCBIfam TIGR02483; PFK_mixed; 1;
PROSITE PS00433; PHOSPHOFRUCTOKINASE; 1;

Features [?]

From: PFP_AMYME (Q59126)
Key From To Description Tag Condition FTGroup
SITE 104 104 /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" PPI D
SITE 104 104 /note="Important for substrate specificity; cannot use PPi as phosphoryl donor" ATP G
BINDING 125 127 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 T-x-D
BINDING 169 171 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 M-G-[RH]
BINDING 271 274 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 [HY]-x(2)-R
ACT_SITE 127 127 /note="Proton acceptor" D
BINDING 103 103 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_note="catalytic"		 [DEN]
BINDING 162 162 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"		 R
BINDING 221 221 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 E
BINDING 265 265 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"		 [RK]
case <FTTag:PPI>
BINDING 10 10 /ligand="diphosphate"
/ligand_id="ChEBI:CHEBI:33019"		 G
SITE 124 124 /note="Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi" K
end case
From: PFKA2_STRCO (Q9L1L8)
Key From To Description Tag Condition FTGroup
case <FTTag:ATP>
BINDING 72 73 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [RK]-x
BINDING 102 105 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G-[DEN]-G-[ST]
BINDING 10 10 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G
end case

Additional information [?]

Size range 336-384 amino acids
Related rules None
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-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.



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