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    ilvB acetohydroxy acid synthase I subunit IlvB [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948182, updated on 3-Dec-2024

    Summary

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    Official Symbol
    ilvB
    Official Full Name
    acetohydroxy acid synthase I subunit IlvB
    Primary source
    ECOCYC:EG10494
    Locus tag
    b3671
    See related
    ASAP:ABE-0011999
    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
    ECK3662
    Summary
    Bifunctional acetohydroxybutanoate synthase / acetolactate synthase (IlvB/N) carries out both the first step in valine biosynthesis and the second step in isoleucine biosynthesis. [More information is available at EcoCyc: EG10494].
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    Genomic context

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    Sequence:
    NC_000913.3 (3851096..3852784, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene sensory histidine kinase UhpB Neighboring gene DNA-binding transcriptional activator UhpA Neighboring gene acetohydroxy acid synthase I subunit IlvN Neighboring gene ilvBN operon leader peptide Neighboring gene ncRNA

    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. Plasmid-associated functions of a stable Flac. Macrina FL, et al. J Bacteriol, 1973 Jan. PMID 4569402, Free PMC Article
    2. Nucleotide sequence of the ilvB multivalent attenuator region of Escherichia coli K12. Hauser CA, et al. Nucleic Acids Res, 1983 Jan 11. PMID 6346263, Free PMC Article
    3. Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme. Mitra A, et al. Biochemistry, 2008 Feb 12. PMID 18193896
    4. Acetohydroxy acid synthase I of Escherichia coli: purification and properties. Grimminger H, et al. J Bacteriol, 1979 Feb. PMID 370104, Free PMC Article
    5. Role of small subunit (IlvN polypeptide) of acetohydroxyacid synthase I from Escherichia coli K-12 in sensitivity of the enzyme to valine inhibition. Eoyang L, et al. J Bacteriol, 1986 Jun. PMID 3011751, Free PMC Article

    See all (45) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 acetolactate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables acetolactate synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables acetolactate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables flavin adenine dinucleotide binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables flavin adenine dinucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables thiamine pyrophosphate binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transferase activity 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
    		  
    acts_upstream_of_or_within L-valine biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in L-valine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in amino acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in branched-chain amino acid biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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
    		  
    acts_upstream_of_or_within isoleucine biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in isoleucine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    part_of acetolactate synthase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of acetolactate synthase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of acetolactate synthase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    acetohydroxy acid synthase I subunit IlvB
    NP_418127.1

    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
      3851096..3852784 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418127.1 acetohydroxy acid synthase I subunit IlvB [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418127.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376FV27, A0A828NVH1, A0A8S7F8F1, A0A8S7TK91
      Conserved Domains (1) summary
      PRK08155
      Location:1 → 562
      PRK08155; acetolactate synthase large subunit
    Nucleotide Protein
    Heading Accession and Version

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