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HAMAP rule MF_01979

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General rule information [?]

Accession MF_01979
Dates 16-MAY-2014 (Created)
19-NOV-2022 (Last updated, Version 11)
Name Phosphofructokinase_II_Short
Scope(s) Bacteria
Template(s) Q9WYC5 (PFP_THEMA); Q27705 (PFP_NAEFO); A2E9H3 (PFP2_TRIV3); [ Recover all ]
Triggered by HAMAP; MF_01979 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PFP
Protein name RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase;
AltName: Full=6-phosphofructokinase, pyrophosphate dependent;
AltName: Full=PPi-dependent phosphofructokinase;
AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase;
case <OC:Bacteria>
Gene name Name=pfp;
end case

Comments [?]

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 + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
PATHWAYCarbohydrate degradation; glycolysis; D-glyceraldehyde 3- phosphate and glycerone phosphate from D-glucose: step 3/4.
case <OC:Bacteria>
else case <OC:Eukaryota>
end case
SIMILARITYBelongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily.

Keywords [?]

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 PIRSF036482; PPi_PFK_TM0289; 1;

Features [?]

Key From To Description Tag Condition FTGroup
SITE 108 108 /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" D
BINDING 132 134 /ligand="substrate" T-x-D
BINDING 178 180 /ligand="substrate" M-G-R
BINDING 300 303 /ligand="substrate" Y-x(2)-R
ACT_SITE 134 134 /note="Proton acceptor" D
BINDING 107 107 /ligand="Mg(2+)"
BINDING 238 238 /ligand="substrate" E
BINDING 12 12 /ligand="diphosphate"
SITE 131 131 /note="Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi" K

Additional information [?]

Size range 411-476 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).

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