U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

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

Gene ID: 948138, updated on 10-Oct-2024

Summary

Go to the top of the page Help
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
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
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

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

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

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

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

Go to the top of the page Help
Preferred Names
2-amino-3-ketobutyrate CoA ligase
NP_418074.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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, A0AAN5FAE3
    Conserved Domains (1) summary
    PRK06939
    Location:1 → 397
    PRK06939; 2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.