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    codA cytosine/isoguanine deaminase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944996, updated on 17-Dec-2024

    Summary

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    Official Symbol
    codA
    Official Full Name
    cytosine/isoguanine deaminase
    Primary source
    ECOCYC:EG11326
    Locus tag
    b0337
    See related
    ASAP:ABE-0001161
    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
    ECK0334
    Summary
    Earlier characterization of the enzyme had found it to consist of two polypeptides of different molecular mass. [More information is available at EcoCyc: EG11326].
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    Genomic context

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    Sequence:
    NC_000913.3 (356171..357454)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene 2-methylcitrate dehydratase Neighboring gene propionyl-CoA synthetase Neighboring gene cytosine transporter Neighboring gene DNA-binding transcriptional dual regulator CynR Neighboring gene carbonic anhydrase 1

    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. Transfer of the bacterial gene for cytosine deaminase to mammalian cells confers lethal sensitivity to 5-fluorocytosine: a negative selection system. Mullen CA, et al. Proc Natl Acad Sci U S A, 1992 Jan 1. PMID 1729703, Free PMC Article
    2. The structure of Escherichia coli cytosine deaminase. Ireton GC, et al. J Mol Biol, 2002 Jan 25. PMID 11812140
    3. Genetic selection scheme for isolation of signal transduction pathway mutants. Anandan S, et al. Appl Environ Microbiol, 2004 Feb. PMID 14766578, Free PMC Article
    4. Deamination of isoguanine by Escherichia coli. FRIEDMAN S, et al. Arch Biochem Biophys, 1951 Jun. PMID 14847690
    5. Alanine-scanning mutagenesis reveals a cytosine deaminase mutant with altered substrate preference. Mahan SD, et al. Biochemistry, 2004 Jul 20. PMID 15248753

    See all (34) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Data show that peptide deformylase, threonine dehydrogenase, and cytosine deaminase are very sensitve to hydrogen peroxide.
      Title: Mononuclear iron enzymes are primary targets of hydrogen peroxide stress.
    2. N-terminus verified by Edman degradation on mature peptide
      Title: Characterization of the Escherichia coli codBA operon encoding cytosine permease and cytosine deaminase.
    3. Future therapeutic local application of cell-permeable cytosine deaminase-TLM fusion proteins together with a systemic fluorouracil prodrug application could result in profound hepatoma antitumor activities without apparent side effects.
      Title: Protein transduction with bacterial cytosine deaminase fused to the TLM intercellular transport motif induces profound chemosensitivity to 5-fluorocytosine in human hepatoma cells.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    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 cytosine deaminase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables cytosine deaminase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables cytosine deaminase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ferrous iron binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds 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 isoguanine deaminase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables isoguanine deaminase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables isoguanine deaminase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cytosine catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within cytosine catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in cytosine metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytosol HDA PubMed 

    General protein information

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    Preferred Names
    cytosine/isoguanine deaminase
    NP_414871.1

    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
      356171..357454
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414871.1 cytosine/isoguanine deaminase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414871.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2W6NWD8
      Conserved Domains (1) summary
      PRK09230
      Location:2 → 427
      PRK09230; cytosine deaminase; Provisional
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

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    Other Literature Sources
    Molecular Biology Databases
    Research Materials