U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

birA DNA-binding transcriptional repressor/biotin- [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948469, updated on 30-Jul-2025
Official Symbol
birA
Official Full Name
DNA-binding transcriptional repressor/biotin-
Primary source
ECOCYC:EG10123
Locus tag
b3973
See related
ASAP:ABE-0013001
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
bioR; dhbB; ECK3965
Summary
Biotinyl-5'-AMP is the co-repressor and is also synthesized by BirA (Cronan, 1988). [More information is available at EcoGene: EG10123]. BirA is a bifunctional protein that exhibits biotin ligase activity and also acts as the DNA binding transcriptional repressor of the biotin operon . [More information is available at EcoCyc: EG10123].
NEW
Try the new Gene table
Try the new Transcript table
Sequence:
NC_000913.3 (4173082..4174047)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene 23S ribosomal RNA Neighboring gene 5S ribosomal RNA Neighboring gene UDP-N-acetylenolpyruvoylglucosamine reductase Neighboring gene pantothenate kinase Neighboring gene tRNA-Thr

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. In vitro enzymatic biotinylation of recombinant fab fragments through a peptide acceptor tail. Saviranta P, et al. Bioconjug Chem, 1998 Nov-Dec. PMID 9815166
  2. Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis. Xu Y, et al. Biochemistry, 1995 Dec 26. PMID 8527435
  3. Structural similarities in the noncatalytic domains of phenylalanyl-tRNA and biotin synthetases. Safro M, et al. Protein Sci, 1995 Nov. PMID 8563641, Free PMC Article
  4. Thermodynamic analysis of small ligand binding to the Escherichia coli repressor of biotin biosynthesis. Xu Y, et al. Biochemistry, 1996 Apr 30. PMID 8611542
  5. Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant. Xu Y, et al. Biochemistry, 1996 Feb 13. PMID 8639659

See all (105) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. A conserved regulatory mechanism in bifunctional biotin protein ligases BirA has been demonstrated for three bacterial strains.
    Title: A conserved regulatory mechanism in bifunctional biotin protein ligases.
  2. BirA signals to the global regulator Fur, which in turn activates LEE (locus of enterocyte effacement) genes to promote EHEC adherence in the low-biotin large intestine.
    Title: Enterohemorrhagic Escherichia coli senses low biotin status in the large intestine for colonization and infection.
  3. work demonstrates that variable surface loops evolved to support BirA function in the homodimerization required for transcription repression by complementing the constant loops, which are constrained because of their essential role in posttranslational biotin addition
    Title: Functional versatility of a single protein surface in two protein:protein interactions.
  4. BirA function entails extensive interactions among the three domains of the protein and show that normal ligase activity does not ensure normal DNA binding.
    Title: Altered regulation of Escherichia coli biotin biosynthesis in BirA superrepressor mutant strains.
  5. energetic and structural underpinnings of the dual specificity of protein BirA as a homodimer or as a heterodimer with acetyl coenzyme A carboxylase
    Title: Thermodynamic and structural investigation of bispecificity in protein-protein interactions.
  6. BirA ligase biotinylates K4, K9, K18 and K23 in histone H3.
    Title: Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3.
  7. Results indicate that the hydrophobic cluster is critical to the ligand-induced disorder-to-order transition in birA and that this transition is integral to the allosteric response in the biotin repressor.
    Title: Nucleation of an allosteric response via ligand-induced loop folding.
  8. Results describe the 2.8A resolution crystal structure of BirA in complex with the co-repressor analog biotinol-5'-AMP.
    Title: Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables DNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables DNA binding IEA
Inferred from Electronic Annotation
more info
  
enables biotin binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables biotin binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables biotin--[biotin carboxyl-carrier protein] ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables biotin--[biotin carboxyl-carrier protein] ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables biotin--[biotin carboxyl-carrier protein] ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables nucleic acid binding EXP
Inferred from Experiment
more info
 PubMed 
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein homodimerization activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables transcription cis-regulatory region binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within biotin biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in biotin metabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of DNA-templated transcription IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of transcription repressor complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of transcription repressor complex IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Preferred Names
DNA-binding transcriptional repressor/biotin-
NP_418404.1

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
    4173082..4174047
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418404.1 DNA-binding transcriptional repressor/biotin-[acetyl-CoA-carboxylase] ligase BirA

    See identical proteins and their annotated locations for NP_418404.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A8S7EPH2, A0AAN5ZLZ2
    Conserved Domains (1) summary
    PRK11886
    Location:2 → 320
    PRK11886; bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA
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.