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    ilvC ketol-acid reductoisomerase (NADP(+)) [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948286, updated on 3-Dec-2024

    Summary

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    Official Symbol
    ilvC
    Official Full Name
    ketol-acid reductoisomerase (NADP(+))
    Primary source
    ECOCYC:EG10495
    Locus tag
    b3774
    See related
    ASAP:ABE-0012331
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK3766
    Summary
    Acetohydroxy acid isomeroreductase (IlvC) carries out two analogous keto-acid reductoisomerase reactions in the parallel biosynthetic pathways generating isoleucine and valine. [More information is available at EcoCyc: EG10495].
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    Genomic context

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    Sequence:
    NC_000913.3 (3957970..3959445)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene threonine deaminase Neighboring gene DNA-binding transcriptional dual regulator IlvY Neighboring gene peptidyl-prolyl cis-trans isomerase C Neighboring gene pseudo

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Absence of significant membrane localization of the proteins coded by the ilvGEDAC genes of Escherichia coli K-12. Gray JE, et al. J Bacteriol, 1982 Jul. PMID 6211429, Free PMC Article
    2. Reversal of the nucleotide specificity of ketol acid reductoisomerase by site-directed mutagenesis identifies the NADPH binding site. Rane MJ, et al. Arch Biochem Biophys, 1997 Feb 1. PMID 9015391
    3. Purified recombinant Escherichia coli ketol-acid reductoisomerase is unsuitable for use in a coupled assay of acetohydroxyacid synthase activity due to an unexpected side reaction. Hill CM, et al. Protein Expr Purif, 1999 Feb. PMID 10024470
    4. Isoleucine and valine metabolism of Escherichia coli. I. Growth studies on amino acid-deficient mutants. UMBARGER HE, et al. J Biol Chem, 1951 Mar. PMID 14832239
    5. Facile crystallization of Escherichia coli ketol-acid reductoisomerase. McCourt JA, et al. Acta Crystallogr D Biol Crystallogr, 2004 Aug. PMID 15272168

    See all (44) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Key cofactor specificity determinants are identified and five enzymes constructed with reversed cofactor preference; additional directed evolution generated two enzymes with NADH-dependent catalytic efficiencies greater than wild-type enzymes with NADPH.
      Title: General approach to reversing ketol-acid reductoisomerase cofactor dependence from NADPH to NADH.
    2. Ultracentrifugation studies confirm that the enzyme exists as a tetramer in solution, and isothermal titration calorimetry shows that the binding of Mg(2+) decreases, while the binding of NADPH increases the structural rigidity of the enzyme.
      Title: Bacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycle.
    3. N-terminus verified by Edman degradation on mature peptide
      Title: '98 Escherichia coli SWISS-2DPAGE database update.
    4. crystal structure of Escherichia coli ketol-acid reductoisomerase
      Title: Facile crystallization of Escherichia coli ketol-acid reductoisomerase.
    5. crystal structure of the E. coli enzyme at 2.6 A resolution, the first three-dimensional structure of any bacterial Class II KARI
      Title: The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables 2-dehydropantoate 2-reductase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables NADP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ketol-acid reductoisomerase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ketol-acid reductoisomerase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ketol-acid reductoisomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in L-valine biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in L-valine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within L-valine biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in amino acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in branched-chain amino acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in isoleucine biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in isoleucine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within isoleucine biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within pantothenate biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of protein-containing complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    ketol-acid reductoisomerase (NADP(+))
    NP_418222.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      3957970..3959445
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418222.1 ketol-acid reductoisomerase (NADP(+)) [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418222.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9ARA2
      Conserved Domains (1) summary
      PRK05225
      Location:2 → 488
      PRK05225; ketol-acid reductoisomerase; Validated
    Nucleotide Protein
    Heading Accession and Version

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