HAMAP rule MF_03186
General rule information
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Accession | MF_03186 |
Dates | 16-MAY-2014 (Created) 19-NOV-2022 (Last updated, Version 12) |
Name | Phosphofructokinase_II_X_euk |
Scope | Eukaryota |
Templates | O15648 (PFKA_TRYBB); Q27651 (PFKA_ENTH1); Q9BIC6 (PFKA_LEIDO); Q4E657 (PFKA_TRYCC): [Recover all] |
case <OC:Eukaryota>
Triggered by |
end case
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
case <OC:Viridiplantae>
Gene name |
|
else case <OC:Kinetoplastea>
Gene name |
|
end case
Comments
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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 AMP. |
Pathway | Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. |
Subunit | Homotetramer. |
case <OC:Kinetoplastea>
Subcellular location | Glycosome. |
else
Subcellular location | Cytoplasm. |
end case
Similarity | Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily. |
Keywords
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Allosteric enzyme
Kinase
Transferase
Glycolysis
ATP-binding
Nucleotide-binding
Magnesium
Metal-binding
Kinase
Transferase
Glycolysis
ATP-binding
Nucleotide-binding
Magnesium
Metal-binding
case <OC:Kinetoplastea>
else
end case
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 | PIRSF000534; PPi_PFK_TP0108; 1; |
PRINTS | PR00476; PHFRCTKINASE; 1; |
Features
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From: PFKA_TRYBB (O15648) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
SITE (Optional) | 200 | 200 | Important for substrate specificity; cannot use PPi as phosphoryl donor | G | ||||||||
BINDING | 173 | 174 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | [RK]-x | ||||||||
BINDING | 198 | 201 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | G-[DENG]-G-[ST] | ||||||||
BINDING | 107 | 107 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | G | ||||||||
BINDING | 227 | 229 | /ligand="substrate | T-x-D | ||||||||
BINDING | 272 | 274 | /ligand="substrate | M-G-[RH] | ||||||||
BINDING | 380 | 383 | /ligand="substrate | [HY]-x(2)-R | ||||||||
ACT_SITE | 229 | 229 | Proton acceptor | D | ||||||||
BINDING | 199 | 199 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="catalytic | [DEN] | ||||||||
BINDING | 325 | 325 | /ligand="substrate | E |
case <OC:Kinetoplastea>
end case
Additional information
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Size range | 436-537 amino acids |
Related rules | MF_01981 (PFKA) |
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). |