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HAMAP rule MF_01980

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General rule information [?]

Accession MF_01980
Dates 16-MAY-2014 (Created)
1-JUN-2023 (Last updated, Version 13)
Name Phosphofructokinase_II_Long
Scope(s) Bacteria
Template(s) P70826 (PFP_BORBU); C4LZC2 (PFP_ENTH1); [ Recover all ]
Triggered by
case c? <OC:Bacteria>
HAMAP; MF_01980 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

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;
Gene name Name=pfp;
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;
Gene name Name=pfkA;
else
Identifier PFKA
Protein name RecName: Full=6-phosphofructokinase;
                 EC=2.7.1.-;
Gene name Name=pfk;
end case

Comments [?]

case <FT:1>
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=2.7.1.90;
ACTIVITY REGULATIONNon-allosteric.
else case <FT:2>
FUNCTIONCatalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
CATALYTIC ACTIVITY Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6- bisphosphate + 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.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.

Keywords [?]

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;
NCBIfam TIGR02477; PFKA_PPi; 1;

Features [?]

From: PFP_BORBU (P70826)
Key From To Description Tag Condition FTGroup
SITE 177 177 /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
SITE 177 177 /note="Important for substrate specificity; cannot use PPi as phosphoryl donor" G
case <FT:1>
BINDING 82 82 /ligand="diphosphate"
/ligand_id="ChEBI:CHEBI:33019"		 G
SITE 203 203 /note="Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi" K
else case <FT:2>
BINDING 146 147 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [RK]-x
BINDING 175 178 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G-[DE]-G-[ST]
BINDING 82 82 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G
end case
case <FT:1> or <FT:2>
BINDING 204 206 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 T-x-D
BINDING 243 244 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"		 K-Y
BINDING 251 253 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 M-G-[RH]
BINDING 428 431 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 [HY]-x(2)-R
ACT_SITE 206 206 /note="Proton acceptor" D
BINDING 176 176 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_note="catalytic"		 [DE]
BINDING 312 312 /ligand="substrate"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"		 E
end case

Additional information [?]

Size range 548-573 amino acids
Related rules MF_03185
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-177 (PFP_BORBU 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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