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HAMAP rule MF_00339

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General rule information [?]

Accession MF_00339
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 45)
Name Phosphofructokinase_I_B1
Scope
Bacteria
Templates P0A796 (PFKA_ECOLI); P00512 (PFKA_GEOSE); P0DOB6 (PFKA1_LACLL); Q9WY52 (PFKA_THEMA); P21777 (PFKA1_THET8): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

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

Comments [?]

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
Cofactor Mg(2+)
Activity regulation Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.
Pathway Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subunit Homotetramer.
Subcellular location Cytoplasm.
Similarity Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily.

Keywords [?]

Allosteric enzyme
Cytoplasm
Kinase
Transferase
Glycolysis
ATP-binding
Nucleotide-binding
Magnesium
Metal-binding

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 TIGR02482; PFKA_ATP; 1;
PROSITE PS00433; PHOSPHOFRUCTOKINASE; 1;

Features [?]

From: PFKA_ECOLI (P0A796)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     73     74       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     R-x  
BINDING     103     106       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     G-[DEN]-G-[ST]  
BINDING     22     26       /ligand="ADP" /ligand_id="ChEBI:CHEBI:456216" /ligand_note="allosteric activator; ligand shared between dimeric partners     R-x(3)-[RK]  
BINDING (Optional)     55     60       /ligand="ADP" /ligand_id="ChEBI:CHEBI:456216" /ligand_note="allosteric activator; ligand shared between dimeric partners     R-Y-x(2)-S-[DE]  
BINDING     126     128       /ligand="substrate" /ligand_note="ligand shared between dimeric partners" /note="in other chain     [TS]-x-D  
BINDING     170     172       /ligand="substrate" /ligand_note="ligand shared between dimeric partners" /note="in other chain     M-G-[RHN]  
BINDING     186     188       /ligand="ADP" /ligand_id="ChEBI:CHEBI:456216" /ligand_note="allosteric activator; ligand shared between dimeric partners" /note="in other chain     G-x-[ED]  
BINDING     214     216       /ligand="ADP" /ligand_id="ChEBI:CHEBI:456216" /ligand_note="allosteric activator; ligand shared between dimeric partners" /note="in other chain     K-x(2)  
BINDING     250     253       /ligand="substrate" /ligand_note="ligand shared between dimeric partners" /note="in other chain     [HY]-x(2)-R  
ACT_SITE     128     128       Proton acceptor     D  
BINDING     104     104       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="catalytic     [DEN]  
BINDING     12     12       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     G  
BINDING     155     155       /ligand="ADP" /ligand_id="ChEBI:CHEBI:456216" /ligand_note="allosteric activator; ligand shared between dimeric partners" /note="in other chain     [RK]  
BINDING     163     163       /ligand="substrate" /ligand_note="ligand shared between dimeric partners     R  
BINDING (Optional)     212     212       /ligand="ADP" /ligand_id="ChEBI:CHEBI:456216" /ligand_note="allosteric activator; ligand shared between dimeric partners" /note="in other chain     [RK]  
BINDING     223     223       /ligand="substrate" /ligand_note="ligand shared between dimeric partners" /note="in other chain     E  
BINDING     244     244       /ligand="substrate" /ligand_note="ligand shared between dimeric partners     [RK]  

Additional information [?]

Size range 319-361 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).


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