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    kbl 2-amino-3-ketobutyrate CoA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948138, updated on 17-Dec-2024

    Summary

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    Official Symbol
    kbl
    Official Full Name
    2-amino-3-ketobutyrate CoA ligase
    Primary source
    ECOCYC:EG10512
    Locus tag
    b3617
    See related
    ASAP:ABE-0011832
    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
    ECK3607
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    Genomic context

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    Sequence:
    NC_000913.3 (3791355..3792551, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene divergent polysaccharide deacetylase domain-containing protein YibQ Neighboring gene UDP-glucuronate:LPS(HepIII) glycosyltransferase Neighboring gene threonine dehydrogenase Neighboring gene protein HtrL Neighboring gene ADP-L-glycero-D-mannoheptose 6-epimerase

    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. Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes. Bashir Q, et al. Chem Commun (Camb), 2006 Dec 28. PMID 17146529
    2. Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism. Schmidt A, et al. Biochemistry, 2001 May 1. PMID 11318637
    3. 2-Amino-3-ketobutyrate CoA ligase of Escherichia coli: stoichiometry of pyridoxal phosphate binding and location of the pyridoxyllysine peptide in the primary structure of the enzyme. Mukherjee JJ, et al. Biochim Biophys Acta, 1990 Jan 19. PMID 2104756
    4. Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase. Marcus JP, et al. J Bacteriol, 1993 Oct. PMID 8407827, Free PMC Article
    5. The role of H-NS in one carbon metabolism. Landgraf JR, et al. Biochimie, 1994. PMID 7748928

    See all (16) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on complete protein
      Title: Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme.
    2. The condensation process catalysed by 2-amino-3-ketobutyrate ligase (KBL; also known as 2-amino-3-ketobutyrate ligase) involves the loss of the pro-R hydrogen atom of glycine and occurs with the inversion of stereochemistry.
      Title: Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes.
    Submit: New GeneRIF Correction

    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 acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables catalytic activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glycine C-acetyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables glycine C-acetyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glycine C-acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables pyridoxal phosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables pyridoxal phosphate binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in L-threonine catabolic process to glycine IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in threonine catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    2-amino-3-ketobutyrate CoA ligase
    NP_418074.1

    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
      3791355..3792551 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418074.1 2-amino-3-ketobutyrate CoA ligase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418074.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7BZX9
      Conserved Domains (1) summary
      PRK06939
      Location:1 → 397
      PRK06939; 2-amino-3-ketobutyrate coenzyme A ligase; Provisional
    Nucleotide Protein
    Heading Accession and Version

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