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

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: REVIEWED
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadati; 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_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
Two crystal forms of Escherichia coli tryptophanase.
Title: Structures of Escherichia coli tryptophanase in holo and 'semi-holo' forms.
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.
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.
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.
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.
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.
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

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables L-cysteine desulfhydrase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables carbon-carbon lyase 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	IBA Inferred from Biological aspect of Ancestor more info
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 L-tryptophan catabolic process	IEA Inferred from Electronic Annotation more info
involved_in L-tryptophan catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in L-tryptophan metabolic process	IEA Inferred from Electronic Annotation more info
involved_in amino acid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in aromatic amino acid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in indole metabolic process	IDA Inferred from Direct Assay more info	PubMed

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 more info	PubMed
located_in membrane	HDA more info	PubMed
part_of protein-containing complex	IDA Inferred from Direct Assay more info	PubMed