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    gltA citrate synthase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945323, updated on 3-Dec-2024

    Summary

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    Official Symbol
    gltA
    Official Full Name
    citrate synthase
    Primary source
    ECOCYC:EG10402
    Locus tag
    b0720
    See related
    ASAP:ABE-0002451
    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
    ECK0709; gluT; icdB
    Summary
    The Escherichia coli citrate synthase is a type II enzyme, which appears to be unique to the Gram-negative bacteria. [More information is available at EcoCyc: EG10402].
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    Genomic context

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    Sequence:
    NC_000913.3 (753185..754468, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative fimbrial usher protein YbgQ Neighboring gene putative fimbrial protein YbgD Neighboring gene protein YbgV Neighboring gene protein YbgU Neighboring gene succinate:quinone oxidoreductase, membrane protein SdhC Neighboring gene succinate:quinone oxidoreductase, membrane protein SdhD

    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. Characterization of rate-controlling steps in vivo by use of an adjustable expression vector. Walsh K, et al. Proc Natl Acad Sci U S A, 1985 Jun. PMID 3889909, Free PMC Article
    2. Active site mutants of Escherichia coli citrate synthase. Effects of mutations on catalytic and allosteric properties. Pereira DS, et al. J Biol Chem, 1994 Jan 7. PMID 8276829
    3. Regulation of the citrate synthase (gltA) gene of Escherichia coli in response to anaerobiosis and carbon supply: role of the arcA gene product. Park SJ, et al. J Bacteriol, 1994 Aug. PMID 8051021, Free PMC Article
    4. icdB mutants of Escherichia coli. Helling RB. J Bacteriol, 1995 May. PMID 7730298, Free PMC Article
    5. The binding of propionyl-CoA and carboxymethyl-CoA to Escherichia coli citrate synthase. Man WJ, et al. Biochim Biophys Acta, 1995 Jul 3. PMID 7612655

    See all (58) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Engineered citrate synthase alters Acetate Accumulation in Escherichia coli.
      Title: Engineered citrate synthase alters Acetate Accumulation in Escherichia coli.
    2. GltA, icd and mdh do not form a transcription unit, are scattered around the chromosome and are expressed from different promoters.
      Title: Interaction of enzymes of the tricarboxylic acid cycle in Bacillus subtilis and Escherichia coli: a comparative study.
    3. N-terminus verified by Edman degradation on mature peptide
      Title: Changes in protein synthesis as a consequence of heme depletion in Escherichia coli.
    4. For citrate synthase the change in the number of interdomain contacting atoms upon closure remained largely the same, suggesting that the domain faces slide over each other during closure
      Title: Essential dynamics sampling study of adenylate kinase: comparison to citrate synthase and implication for the hinge and shear mechanisms of domain motions.
    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 NADH binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables acyltransferase activity, acyl groups converted into alkyl on transfer IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables citrate (Si)-synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables citrate (Si)-synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables citrate (Si)-synthase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables citrate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within protein hexamerization IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in tricarboxylic acid cycle IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    citrate synthase
    NP_415248.1

    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
      753185..754468 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415248.1 citrate synthase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415248.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376FSH9, A0A376MTP3, A0A5B9AK54
      Conserved Domains (1) summary
      PRK05614
      Location:1 → 416
      gltA; citrate synthase
    Nucleotide Protein
    Heading Accession and Version

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