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    tnaA tryptophanase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948221, updated on 26-Nov-2024

    Summary

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    Official Symbol
    tnaA
    Official Full Name
    tryptophanase
    Primary source
    ECOCYC:EG11005
    Locus tag
    b3708
    See related
    ASAP:ABE-0012133
    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
    ECK3701; ind; tnaR
    Summary
    TnaA is required for growth on tryptophan as a carbon source and indole as a tryptophan source. [More information is available at EcoGene: EG11005]. Several distinct proteins exhibit cysteine desulfhydrase activity, which is involved in cysteine degradation . [More information is available at EcoCyc: EG11005].
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    Genomic context

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    Sequence:
    NC_000913.3 (3888730..3890145)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene 5-carboxymethylaminomethyluridine-tRNA synthase GTPase subunit Neighboring gene tnaAB operon leader peptide Neighboring gene tryptophan:H(+) symporter TnaB Neighboring gene efflux pump MdtL Neighboring gene DNA-binding transcriptional dual regulator YidZ

    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 tryptophanase from Escherichia coli K-12. I. Purification, physical properties, and quaternary structure. London J, et al. J Biol Chem, 1972 Mar 10. PMID 4551942
    2. GENETIC ANALYSIS OF TRYPTOPHANASE MUTANTS OF ESCHERICHIA COLI. GARTNER TK, et al. J Bacteriol, 1965 Feb. PMID 14255697, Free PMC Article
    3. Properties of tryptophanase from Escherichia coli. BURNS RO, et al. Biochim Biophys Acta, 1962 Dec 4. PMID 14017164
    4. Indole can act as an extracellular signal to regulate biofilm formation of Escherichia coli and other indole-producing bacteria. Martino PD, et al. Can J Microbiol, 2003 Jul. PMID 14569285
    5. Selection of mutants of Escherichia coli constitutive for tryptophanase. NG H, et al. J Bacteriol, 1963 Jan. PMID 13938299, Free PMC Article

    See all (66) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Posttranscriptional Regulation of tnaA by Protein-RNA Interaction Mediated by Ribosomal Protein L4 in Escherichia coli.
      Title: Posttranscriptional Regulation of tnaA by Protein-RNA Interaction Mediated by Ribosomal Protein L4 in Escherichia coli.
    2. A structural view of the dissociation of Escherichia coli and Proteus vulgaris tryptophanase subunits has been presented.
      Title: A structural view of the dissociation of Escherichia coli tryptophanase.
    3. The results suggest that TnaA activity is regulated by subcellular localization and by a loop-associated occlusion of its active site.
      Title: A new suite of tnaA mutants suggests that Escherichia coli tryptophanase is regulated by intracellular sequestration and by occlusion of its active site.
    4. Two crystal forms of Escherichia coli tryptophanase.
      Title: Structures of Escherichia coli tryptophanase in holo and 'semi-holo' forms.
    5. In addition, adding glucose and other carbohydrates rapidly inhibited the function of pre-formed TnaA, indicating that TnaA is regulated by a previously unknown carbohydrate-dependent post-translational mechanism.
      Title: A cAMP-independent carbohydrate-driven mechanism inhibits tnaA expression and TnaA enzyme activity in Escherichia coli.
    6. The results imply that Escherichia coli synthesizes TnaA and TnaB mainly, or solely, for the purpose of converting exogenous tryptophan into indole, under conditions and for signalling purposes that remain to be fully elucidated.
      Title: Indole production by the tryptophanase TnaA in Escherichia coli is determined by the amount of exogenous tryptophan.
    7. The hydrophobic interactions along the non catalytic interface overshadow the effect of point mutations and may account for the differences in the dissociation of E. coli Trpase to dimers.
      Title: Conformational changes and loose packing promote E. coli Tryptophanase cold lability.
    8. Conversion of tryptophan and sodium nitrate into 3-nitrosoindole derivatives requires functional genes for trytophanase (tnaA), a tryptophan permease (tnaB), and a nitrate reductase (narG).
      Title: Production of 3-nitrosoindole derivatives by Escherichia coli during anaerobic growth.
    9. N-terminus verified by Edman degradation on complete protein
      Title: Acid- and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis.
    10. DnaK and DnaJ molecular chaperones apparently influence the amount of tryptophanase, the expression of which is regulated at all transcription steps, including transcription elongation.
      Title: Influence of Escherichia coli DnaK and DnaJ molecular chaperones on tryptophanase (TnaA) amount and GreA, GreB stability.
    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 L-cysteine desulfhydrase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables catalytic 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 lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables potassium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables pyridoxal phosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables tryptophanase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables tryptophanase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tryptophanase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in indole metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in tryptophan catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tryptophan catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tryptophan metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cell pole IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    located_in membrane HDA PubMed 
    part_of protein-containing complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    tryptophanase
    NP_418164.4

    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
      3888730..3890145
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418164.4 tryptophanase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418164.4

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0AAN3TU07
      Conserved Domains (1) summary
      TIGR02617
      Location:5 → 471
      tnaA_trp_ase; tryptophanase, leader peptide-associated
    Nucleotide Protein
    Heading Accession and Version

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