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acnB AcnB [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 944864, updated on 4-Apr-2024

Summary

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Gene symbol
acnB
Gene description
AcnB
Primary source
ASAP:ABE-0000411
Locus tag
b0118
See related
ECOCYC:EG12316
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
ECK0117; yacI; yacJ
Summary
Binds TrxA (Kumar, 2004). [More information is available at EcoGene: EG12316]. Purification of the enzyme is described . [More information is available at EcoCyc: EG12316].
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Genomic context

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Sequence:
NC_000913.3 (131615..134212)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene lipoamide dehydrogenase Neighboring gene DUF3300 domain-containing protein YacH Neighboring gene PF06062 family protein YacL Neighboring gene S-adenosylmethionine decarboxylase proenzyme

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. The iron-sensing aconitase B binds its own mRNA to prevent sRNA-induced mRNA cleavage. Benjamin JA, et al. Nucleic Acids Res, 2014 Sep. PMID 25092924, Free PMC Article
  2. Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation. Tang Y, et al. Mol Microbiol, 2005 Jun. PMID 15882410
  3. E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition. Williams CH, et al. Nat Struct Biol, 2002 Jun. PMID 11992126
  4. Cooperativity of two active sites in bacterial homodimeric aconitases. Tsuchiya D, et al. Biochem Biophys Res Commun, 2009 Feb 6. PMID 19116142
  5. Versatile architecture of a bacterial aconitase B and its catalytic performance in the sequential reaction coupled with isocitrate dehydrogenase. Tsuchiya D, et al. Biochim Biophys Acta, 2008 Nov. PMID 18640291

See all (39) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The data suggest that apo-AcnB protects acnB mRNA from RNase E-mediated cleavage after RyhB pairing.
    Title: The iron-sensing aconitase B binds its own mRNA to prevent sRNA-induced mRNA cleavage.
  2. N-terminus verified by Edman degradation on complete protein
    Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
  3. the N-terminal region of AcnB is necessary and sufficient for promoting the formation of AcnB dimers and also for AcnB binding to target mRNA
    Title: Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables 2-methylisocitrate dehydratase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 2-methylisocitrate dehydratase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 2-methylisocitrate dehydratase activity IEA
Inferred from Electronic Annotation
more info
  
enables 4 iron, 4 sulfur cluster binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 4 iron, 4 sulfur cluster binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables 4 iron, 4 sulfur cluster binding IEA
Inferred from Electronic Annotation
more info
  
enables RNA binding IEA
Inferred from Electronic Annotation
more info
  
enables aconitate hydratase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables aconitate hydratase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables aconitate hydratase activity IEA
Inferred from Electronic Annotation
more info
  
enables iron-sulfur cluster binding IEA
Inferred from Electronic Annotation
more info
  
enables lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables mRNA 3'-UTR binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables mRNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within glyoxylate cycle NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in propionate catabolic process, 2-methylcitrate cycle IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within propionate catabolic process, 2-methylcitrate cycle IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within regulation of translation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in tricarboxylic acid cycle IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in tricarboxylic acid cycle IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within tricarboxylic acid cycle NAS
Non-traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytosol IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
AcnB
NP_414660.1

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
    131615..134212
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414660.1 AcnB [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_414660.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8T6Q1I5, A0AA90ADG5
    Conserved Domains (1) summary
    PRK09238
    Location:1 → 846
    PRK09238; bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Nucleotide Protein
Heading Accession and Version

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