HAMAP rule MF_00339
General rule information
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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
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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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 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
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Allosteric enzyme
Cytoplasm
Kinase
Transferase
Glycolysis
ATP-binding
Nucleotide-binding
Magnesium
Metal-binding
Cytoplasm
Kinase
Transferase
Glycolysis
ATP-binding
Nucleotide-binding
Magnesium
Metal-binding
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 | PIRSF000532; ATP_PFK_prok; 1; |
PRINTS | PR00476; PHFRCTKINASE; 1; |
NCBIfam | TIGR02482; PFKA_ATP; 1; |
PROSITE | PS00433; PHOSPHOFRUCTOKINASE; 1; |
Features
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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
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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). |