trxA thioredoxin 1 [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: trxA
Official Full Name: thioredoxin 1
Primary source: ECOCYC:EG11031
Locus tag: b3781
See related: ASAP:ABE-0012357
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: dasC; ECK3773; fipA; tsnC
Summary: Thioredoxins are small electron-transfer proteins which contain a cysteine disulfide/dithiol active site. [More information is available at EcoCyc: EG11031].
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Genomic context

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Sequence:: NC_000913.3 (3965761..3966090)

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?

Hydrophobic Residue in Escherichia coli Thioredoxin Critical for the Processivity of T7 DNA Polymerase.
Title: Hydrophobic Residue in Escherichia coli Thioredoxin Critical for the Processivity of T7 DNA Polymerase.
By borrowing the CGPC active site of Trx-1 in combination with a T200M point mutation, we transformed DsbG into an enzyme highly reactive toward GSNO and YbiS. The pKa of the nucleophilic cysteine, as well as the redox and thermodynamic properties of the engineered DsbG are dramatically changed and become similar to those of Trx-1.
Title: Sulfur Denitrosylation by an Engineered Trx-like DsbG Enzyme Identifies Nucleophilic Cysteine Hydrogen Bonds as Key Functional Determinant.
In our model, EcTRX folding starts with structure formation in the beta-sheet, while the protein helices coalesce later.
Title: The E. coli thioredoxin folding mechanism: the key role of the C-terminal helix.
Data show that single amino acid mutants require higher detergent concentrations to induce secondary structure than the amount needed for wild type peptide.
Title: Gain of local structure in an amphipathic peptide does not require a specific tertiary framework.
Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.
Title: Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.
analysis of the interaction of the single-stranded DNA-binding protein of bacteriophage T7 with the DNA polymerase-thioredoxin complex
Title: Two modes of interaction of the single-stranded DNA-binding protein of bacteriophage T7 with the DNA polymerase-thioredoxin complex.
Seventeen amino acids clustered around Cys-32 of E. coli thioredoxin 1 is identified as the interaction domain with P. aeruginosa APR. [ARP]
Title: Interaction domain on thioredoxin for Pseudomonas aeruginosa 5'-adenylylsulfate reductase.
Escherichia coli thioredoxin, the processivity factor, binds with bacteriophage T7 DNA polymerase and helicase; first demonstration that thioredoxin interacts with replication proteins other than T7 DNA polymerase
Title: Interactions of Escherichia coli thioredoxin, the processivity factor, with bacteriophage T7 DNA polymerase and helicase.
N-terminus verified by Edman degradation on mature peptide
Title: Thioredoxin. 6. The amino acid sequence of the protein from escherichia coli B.
the structure of PAPS reductase in complex with Trx highlights the large structural rearrangement required to accomplish sulfonucleotide reduction and suggests a role for Trx in catalysis beyond the paradigm of disulfide reduction.
Title: 3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle.

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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 DNA polymerase processivity factor activity	IDA Inferred from Direct Assay more info	PubMed
enables disulfide oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-disulfide reductase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-disulfide reductase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-disulfide reductase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in cell redox homeostasis	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within cell redox homeostasis	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: thioredoxin 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

NC_000913.3 Reference assembly

Range

3965761..3966090

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_418228.2 thioredoxin 1 [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_418228.2

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A5B9AMK3, A0A775TLC9

Conserved Domains (1) summary

PRK09381
Location:1 → 109

trxA; thioredoxin TrxA