HAMAP rule MF_01979
General rule information
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Accession | MF_01979 |
Dates | 16-MAY-2014 (Created) 19-NOV-2022 (Last updated, Version 11) |
Name | Phosphofructokinase_II_Short |
Scope | Bacteria
Eukaryota |
Templates | Q9WYC5 (PFP_THEMA); Q27705 (PFP_NAEFO); A2E9H3 (PFP2_TRIV3): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
case <OC:Bacteria>
Gene name |
|
end case
Comments
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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. |
Cofactor | Mg(2+) |
Pathway | Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. |
case <OC:Bacteria>
Subunit | Homodimer. |
else case <OC:Eukaryota>
Subunit | Homotetramer. |
end case
Subcellular location | Cytoplasm. |
Similarity | Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily. |
Keywords
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Gene Ontology
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GO:0003872; Molecular function: 6-phosphofructokinase activity.
GO:0006096; Biological process: glycolytic process.
GO:0005737; Cellular component: cytoplasm.
GO:0006096; Biological process: glycolytic process.
GO:0005737; Cellular component: cytoplasm.
Cross-references
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Pfam | PF00365; PFK; 1; |
PIRSF | PIRSF036482; PPi_PFK_TM0289; 1; |
PRINTS | PR00476; PHFRCTKINASE; 1; |
Features
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From: PFP_THEMA (Q9WYC5) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
SITE | 108 | 108 | 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 | Proton acceptor | D | ||||||||
BINDING | 107 | 107 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="catalytic | D | ||||||||
BINDING | 238 | 238 | /ligand="substrate | E | ||||||||
BINDING | 12 | 12 | /ligand="diphosphate" /ligand_id="ChEBI:CHEBI:33019 | G | ||||||||
SITE | 131 | 131 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | K |
Additional information
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Size range | 411-476 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). |