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

Gene ID: 948221, updated on 10-Oct-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. Reaction of indole and analogues with amino acid complexes of Escherichia coli tryptophan indole-lyase: detection of a new reaction intermediate by rapid-scanning stopped-flow spectrophotometry. Phillips RS. Biochemistry, 1991 Jun 18. PMID 2043633
  2. The tryptophanase from Escherichia coli K-12. II. Comparison of the thermal stabilities of apo-, holo-, and hybrid enzymes. Raibaud O, et al. J Biol Chem, 1973 May 25. PMID 4573978
  3. Reversibility of the tryptophanase reaction: synthesis of tryptophan from indole, pyruvate, and ammonia. Watanabe T, et al. Proc Natl Acad Sci U S A, 1972 May. PMID 4556453, Free PMC Article
  4. Structure of Escherichia coli tryptophanase. Ku SY, et al. Acta Crystallogr D Biol Crystallogr, 2006 Jul. PMID 16790938
  5. The chemical structure of tryptophanase from Escherichia coli. 3. Isolation and amino acid sequence of the tryptic peptides. Kagamiyama H, et al. J Biol Chem, 1972 Mar 10. PMID 4551944

See all (82) 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.
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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 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
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