trpA tryptophan synthase subunit alpha [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: trpA
Official Full Name: tryptophan synthase subunit alpha
Primary source: ECOCYC:EG11024
Locus tag: b1260
See related: ASAP:ABE-0004232
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: ECK1254; try; tryp
Summary: otherPDB (S. typhimurium): [More information is available at EcoGene: EG11024]. The TrpA polypeptide (TSase ) functions as the subunit of the tetrameric (2-2) tryptophan synthase complex. [More information is available at EcoCyc: EG11024].
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Genomic context

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Sequence:: NC_000913.3 (1316416..1317222, complement)

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?

Allosteric networks intrinsic to alpha tryptophan synthase (alphaTS) are modulated by binding of the beta-subunit to regulate alphaTS function, thus giving insight into coordination of the two active sites.
Title: Long-range interactions in the α subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling.
The conversion of the more stable intermediate to the native state of alpha TS entails the formation of a stable helical shell and completes the acquisition of the tertiary structure.
Title: NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein.
N-terminus verified by Edman degradation on complete protein
Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
protection observed in a contiguous set of beta-strands and alpha-helices in the N terminus implies a significant role for this sub-domain in directing the folding of this TIM barrel protein
Title: An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein.
The molecular origins of the trpA frameshifts analyzed could be explained by one of six simple models based upon misalignment of the template or nascent DNA strands with or without misincorporation of primer nucleotides during DNA replication.
Title: A molecular characterization of spontaneous frameshift mutagenesis within the trpA gene of Escherichia coli.

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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

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables lyase activity	IDA Inferred from Direct Assay more info	PubMed
enables molecular adaptor activity	EXP Inferred from Experiment more info	PubMed
contributes_to tryptophan synthase activity	IDA Inferred from Direct Assay more info	PubMed
enables tryptophan synthase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in L-tryptophan biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in L-tryptophan biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in L-tryptophan biosynthetic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within L-tryptophan biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within aromatic amino acid biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	NAS Non-traceable Author Statement more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed