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The annotation and conditions in this rule are derived from the following entries: P0A796 (PFKA_ECOLI), P00512 (PFKA_GEOSE), P0DOB6 (PFKA1_LACLL), Q9WY52 (PFKA_THEMA), P21777 (PFKA1_THET8)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00339
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 22 - 26 aligns to "R-x(3)-[RK]" in entry P0A796 (individually applies "Allosteric activator ADP binding; shared with dimeric partner")
    • Subsequence at position 73 - 74 aligns to "R-x" in entry P0A796 (individually applies "ATP")
    • Subsequence at position 212 - 212 aligns to "[RK]" in entry P0A796 (individually applies "Allosteric activator ADP")
    • Subsequence at position 128 - 128 aligns to "D" in entry P0A796 (individually applies "Proton acceptor")
    • Subsequence at position 55 - 60 aligns to "R-Y-x(2)-S-[DE]" in entry P0A796 (individually applies "Allosteric activator ADP binding; shared with dimeric partner")
    • Subsequence at position 244 - 244 aligns to "[RK]" in entry P0A796 (individually applies "Substrate; shared with dimeric partner")
    • Subsequence at position 12 - 12 aligns to "G" in entry P0A796 (individually applies "ATP; via amide nitrogen")
    • Subsequence at position 223 - 223 aligns to "E" in entry P0A796 (individually applies "Substrate")
    • Subsequence at position 170 - 172 aligns to "M-G-[RHN]" in entry P0A796 (individually applies "Substrate binding")
    • Subsequence at position 250 - 253 aligns to "[HY]-x(2)-R" in entry P0A796 (individually applies "Substrate binding")
    • Subsequence at position 103 - 106 aligns to "G-[DEN]-G-[ST]" in entry P0A796 (individually applies "ATP")
    • Subsequence at position 155 - 155 aligns to "[RK]" in entry P0A796 (individually applies "Allosteric activator ADP")
    • Subsequence at position 104 - 104 aligns to "[DEN]" in entry P0A796 (individually applies "Magnesium; catalytic")
    • Subsequence at position 214 - 216 aligns to "K-x(2)" in entry P0A796 (individually applies "Allosteric activator ADP binding")
    • Subsequence at position 126 - 128 aligns to "[TS]-x-D" in entry P0A796 (individually applies "Substrate binding")
    • Subsequence at position 186 - 188 aligns to "G-x-[ED]" in entry P0A796 (individually applies "Allosteric activator ADP binding")
    • Subsequence at position 163 - 163 aligns to "R" in entry P0A796 (individually applies "Substrate; shared with dimeric partner")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namei

  • Recommended name:
    ATP-dependent 6-phosphofructokinase (EC:2.7.1.11)
    Short name:
    ATP-PFK
    Short name:
    Phosphofructokinase
    Alternative name(s):
    Phosphohexokinase

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namei

  • Name:pfkA

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

  • Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Homotetramer.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Magnesium; catalytic (to residues corresponding to position 104)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei

  • Proton acceptor (to residues corresponding to position 128)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi

  • ATP (to residues corresponding to positions 73 - 74)
  • ATP (to residues corresponding to positions 103 - 106)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei

  • Allosteric activator ADP (to residues corresponding to position 212)
  • Substrate; shared with dimeric partner (to residues corresponding to position 244)
  • ATP; via amide nitrogen (to residues corresponding to position 12)
  • Substrate (to residues corresponding to position 223)
  • Allosteric activator ADP (to residues corresponding to position 155)
  • Substrate; shared with dimeric partner (to residues corresponding to position 163)

<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • Allosteric activator ADP binding; shared with dimeric partner (to residues corresponding to positions 22 - 26)
  • Allosteric activator ADP binding; shared with dimeric partner (to residues corresponding to positions 55 - 60)
  • Substrate binding (to residues corresponding to positions 170 - 172)
  • Substrate binding (to residues corresponding to positions 250 - 253)
  • Allosteric activator ADP binding (to residues corresponding to positions 214 - 216)
  • Substrate binding (to residues corresponding to positions 126 - 128)
  • Allosteric activator ADP binding (to residues corresponding to positions 186 - 188)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

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