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The annotation and conditions in this rule are derived from the following entries: P16861 (PFKA1_YEAST), P16862 (PFKA2_YEAST), P90521 (PFKA_DICDI), P17858 (PFKAL_HUMAN), P08237 (PFKAM_HUMAN), P00511 (PFKAM_RABIT)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_03184
    • taxon = Eukaryota
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 455 - 455 aligns to "E" in entry P16861 (individually applies "Substrate")
    • Subsequence at position 278 - 279 aligns to "R-x" in entry P16861 (individually applies "ATP")
    • Subsequence at position 488 - 491 aligns to "H-x(2)-R" in entry P16861 (individually applies "Substrate binding")
    • Subsequence at position 859 - 862 aligns to "H-x-Q-Q" in entry P16861 (individually applies "Fructose 2,6-bisphosphate binding; allosteric activator")
    • Subsequence at position 398 - 400 aligns to "M-G-R" in entry P16861 (individually applies "Substrate binding")
    • Subsequence at position 391 - 391 aligns to "R" in entry P16861 (individually applies "Substrate; shared with dimeric partner")
    • Subsequence at position 767 - 769 aligns to "[MQ]-G-[GA]" in entry P16861 (individually applies "Fructose 2,6-bisphosphate binding; allosteric activator")
    • Subsequence at position 581 - 594 aligns to entry P16861 (individually applies "Interdomain linker")
    • Subsequence at position 760 - 760 aligns to "R" in entry P16861 (individually applies "Fructose 2,6-bisphosphate; allosteric activator; shared with dimeric partner")
    • Subsequence at position 952 - 952 aligns to "R" in entry P16861 (individually applies "Fructose 2,6-bisphosphate; allosteric activator")
    • Subsequence at position 595 - @CTER@ aligns to entry P16861 (individually applies "C-terminal regulatory PFK domain 2")
    • Subsequence at position 309 - 309 aligns to "[DE]" in entry P16861 (individually applies "Magnesium; catalytic")
    • Subsequence at position 215 - 215 aligns to "G" in entry P16861 (individually applies "ATP; via amide nitrogen")
    • Subsequence at position 308 - 311 aligns to "G-[DE]-G-[ST]" in entry P16861 (individually applies "ATP")
    • Subsequence at position 853 - 853 aligns to "[RK]" in entry P16861 (individually applies "Fructose 2,6-bisphosphate; allosteric activator; shared with dimeric partner")
    • Subsequence at position 482 - 482 aligns to "[RK]" in entry P16861 (individually applies "Substrate; shared with dimeric partner")
    • Subsequence at position @NTER@ - 580 aligns to entry P16861 (individually applies "N-terminal catalytic PFK domain 1")
    • Subsequence at position 354 - 356 aligns to "S-x-D" in entry P16861 (individually applies "Substrate binding")
    • Subsequence at position 356 - 356 aligns to "D" in entry P16861 (individually applies "Proton acceptor")
    • Subsequence at position 722 - 726 aligns to "[TS]-[ILMV]-S-N-N" in entry P16861 (individually applies "Fructose 2,6-bisphosphate binding; allosteric activator")
    • Subsequence at position 665 - 665 aligns to "[RK]" in entry P16861 (individually applies "Fructose 2,6-bisphosphate; allosteric activator")
    • Subsequence at position 827 - 827 aligns to "[ED]" in entry P16861 (individually applies "Fructose 2,6-bisphosphate; allosteric activator")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Homo- and heterotetramers.
  • Heterooctamer of 4 alpha and 4 beta chains.
  • Homotetramer.

<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%5Fsection">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 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 <a href="http://www.uniprot.org/help/function%5Fsection">'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%5Fsection">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 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 <a href="http://www.uniprot.org/help/function%5Fsection">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 278 - 279)
  • ATP (to residues corresponding to positions 308 - 311)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 356)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 309)

<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

  • Substrate binding (to residues corresponding to positions 488 - 491)
  • Fructose 2,6-bisphosphate binding; allosteric activator (to residues corresponding to positions 859 - 862)
  • Substrate binding (to residues corresponding to positions 398 - 400)
  • Fructose 2,6-bisphosphate binding; allosteric activator (to residues corresponding to positions 767 - 769)
  • Interdomain linker (to residues corresponding to positions 581 - 594)
  • C-terminal regulatory PFK domain 2 (to residues corresponding to positions 595 - @CTER@i)
  • N-terminal catalytic PFK domain 1 (to residues corresponding to positions @NTER@i - 580)
  • Substrate binding (to residues corresponding to positions 354 - 356)
  • Fructose 2,6-bisphosphate binding; allosteric activator (to residues corresponding to positions 722 - 726)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • Substrate (to residues corresponding to position 455)
  • Substrate; shared with dimeric partner (to residues corresponding to position 391)
  • Fructose 2,6-bisphosphate; allosteric activator; shared with dimeric partner (to residues corresponding to position 760)
  • Fructose 2,6-bisphosphate; allosteric activator (to residues corresponding to position 952)
  • ATP; via amide nitrogen (to residues corresponding to position 215)
  • Fructose 2,6-bisphosphate; allosteric activator; shared with dimeric partner (to residues corresponding to position 853)
  • Substrate; shared with dimeric partner (to residues corresponding to position 482)
  • Fructose 2,6-bisphosphate; allosteric activator (to residues corresponding to position 665)
  • Fructose 2,6-bisphosphate; allosteric activator (to residues corresponding to position 827)

<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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