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The annotation and conditions in this rule are derived from the following entries: P05793 (ILVC_ECOLI), Q57179 (ILVC_CORGL), P05989 (ILVC_SALTY), D0WGK0 (ILVC_SLAES), K4LVZ1 (ILVC_THEPS), Q0AV19 (ILVC_SYNWW), B4U6I9 (ILVC_HYDS0), C1DFH7 (ILVC_AZOVD), C8WR67 (ILVC_ALIAD), Q02138 (ILVC_LACLA), P9WKJ7 (ILVC_MYCTU), E0SRA9 (ILVC_IGNAA), O28294 (ILVC_ARCFU), A4YI15 (ILVC_METS5), Q64BR7 (ILVC_UNCAG)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 158 - 158 aligns to "G" in entry P05793 (individually applies "NADP; via amide nitrogen")
    • Subsequence at position 78 - 78 aligns to "[ST]" in entry P05793 (individually applies "NADP")
    • Subsequence at position 414 - 414 aligns to "S" in entry P05793 (individually applies "Substrate")
    • Subsequence at position 108 - 110 aligns to "D-x(1,2)-Q" in entry P05793 (individually applies "NADP")
    • Subsequence at position 221 - 221 aligns to "E" in entry P05793 (individually applies "Magnesium 1")
    • Subsequence at position 389 - 389 aligns to "E" in entry P05793 (individually applies "Magnesium 2")
    • Subsequence at position 393 - 393 aligns to "E" in entry P05793 (individually applies "Magnesium 2")
    • Subsequence at position 76 - 76 aligns to "[RS]" in entry P05793 (individually applies "NADP")
    • Subsequence at position 132 - 132 aligns to "H" in entry P05793 (individually applies "")
    • Subsequence at position 45 - 48 aligns to "[CYF]-G-x-Q" in entry P05793 (individually applies "NADP")
    • Subsequence at position 68 - 68 aligns to "[RK]" in entry P05793 (individually applies "NADP")
    • Subsequence at position 217 - 217 aligns to "D" in entry P05793 (individually applies "Magnesium 1")
    • Subsequence at position 217 - 217 aligns to "D" in entry P05793 (individually applies "Magnesium 2")

... 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

  • Recommended name:
    Ketol-acid reductoisomerase (NADP(+)) (EC:1.1.1.86)
    Short name:
    KARI
    Alternative name(s):
    Acetohydroxy-acid isomeroreductase
    Short name:
    AHIR
    Alpha-keto-beta-hydroxylacyl reductoisomerase

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

<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 <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

  • Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.

<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 '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

  • Pathwayi: L-isoleucine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate. This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.
  • Pathwayi: L-valine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-valine from pyruvate. This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

<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

  • (to residues corresponding to position 132)

<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 1 (to residues corresponding to position 221)
  • Magnesium 2 (to residues corresponding to position 389)
  • Magnesium 2 (to residues corresponding to position 393)
  • Magnesium 1 (to residues corresponding to position 217)
  • Magnesium 2 (to residues corresponding to position 217)

<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

  • NADP (to residues corresponding to positions 108 - 110)
  • NADP (to residues corresponding to positions 45 - 48)

<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

  • NADP; via amide nitrogen (to residues corresponding to position 158)
  • NADP (to residues corresponding to position 78)
  • Substrate (to residues corresponding to position 414)
  • NADP (to residues corresponding to position 76)
  • NADP (to residues corresponding to position 68)

<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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