nrdA ribonucleoside-diphosphate reductase 1 subunit alpha [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

Go to the top of the page Help

Official Symbol: nrdA
Official Full Name: ribonucleoside-diphosphate reductase 1 subunit alpha
Primary source: ECOCYC:EG10660
Locus tag: b2234
See related: ASAP:ABE-0007383
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: dnaF; ECK2226
Summary: Reducing equivalents provided by glutaredoxin or thioredoxin. [More information is available at EcoGene: EG10660]. The B1 protein of ribonucleoside-diphosphate reductase consists of two polypeptide chains of similar or identical size. [More information is available at EcoCyc: EG10660].
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

Sequence:: NC_000913.3 (2344865..2347150)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Elevated Levels of the Escherichia coli nrdAB-Encoded Ribonucleotide Reductase Counteract the Toxicity Caused by an Increased Abundance of the beta Clamp.
Title: Elevated Levels of the Escherichia coli nrdAB-Encoded Ribonucleotide Reductase Counteract the Toxicity Caused by an Increased Abundance of the β Clamp.
Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay.
Title: Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay.
Elimination of 6 helicases lowered NrdA production further, whereas overexpression of any RNA helicase partially reversed the downregulation. UV stress completely reversed down-regulation of NrdA production
Title: REP sequences: Mediators of the environmental stress response?
The present results identifying a large, new set of E. coli mutator strains with mutations of nrdAB ribonucleotide reductase(RNR)confirm the important control that RNR exerts on the cellular mutation rate and provide novel insights into the RNR feedback regulatory mechanisms.
Title: Novel mutator mutants of E. coli nrdAB ribonucleotide reductase: insight into allosteric regulation and control of mutation rates.
RNR101 is unstable at 42 degrees C ; its degradation is prevented by rifampicin; inactivation of DnaA protein by allows chromosome replication in absence of rifampicin and suppresses nucleoid segregation and cell division defects seen in nrdA101 mutant at 42 degrees C
Title: Overlap of replication rounds disturbs the progression of replicating forks in a ribonucleotide reductase mutant of Escherichia coli.
The report three independent methods that establish that Y(356) is the predominant location (85-90%) of the radical, with the remaining 10-15% delocalized onto Y(731) and Y(730) in alpha2.
Title: Equilibration of tyrosyl radicals (Y356•, Y731•, Y730•) in the radical propagation pathway of the Escherichia coli class Ia ribonucleotide reductase.
The authors propose that RecA is required to maintain the integrity of the reversed forks in the nrdA101 mutant under certain restrictive conditions, supporting the relationship between DNA replication and recombination enzymes.
Title: RecA-dependent replication in the nrdA101(Ts) mutant of Escherichia coli under restrictive conditions.
The authors show that the binding of DnaA on the NrdAB promoter can either activate or repress transcription as a function of its concentration and its nucleotide-bound state.
Title: DnaA-ATP acts as a molecular switch to control levels of ribonucleotide reductase expression in Escherichia coli.
N-terminus verified by Edman degradation on complete protein
Title: Protein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotide sequence of the Escherichia coli nrdA gene.
analysis of key residues in the dimerization process of ribonucleotide reductase protein R1
Title: Nucleotide-dependent formation of catalytically competent dimers from engineered monomeric ribonucleotide reductase protein R1.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables ATP binding	IBA Inferred from Biological aspect of Ancestor more info
enables ATP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein folding chaperone	EXP Inferred from Experiment more info	PubMed
contributes_to ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IDA Inferred from Direct Assay more info	PubMed
enables ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IDA Inferred from Direct Assay more info	PubMed
enables ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in 2'-deoxyribonucleotide biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in deoxyribonucleotide biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within deoxyribonucleotide biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in deoxyribonucleotide biosynthetic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within nucleobase-containing small molecule interconversion	IDA Inferred from Direct Assay more info	PubMed
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in ribonucleoside diphosphate metabolic process	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
part_of ribonucleoside-diphosphate reductase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of ribonucleoside-diphosphate reductase complex	IDA Inferred from Direct Assay more info	PubMed
part_of ribonucleoside-diphosphate reductase complex	IPI Inferred from Physical Interaction more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: ribonucleoside-diphosphate reductase 1 subunit alpha

NP_416737.1

EC 1.17.4.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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

2344865..2347150

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_416737.1 ribonucleoside-diphosphate reductase 1 subunit alpha [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_416737.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A780D9R1

Conserved Domains (1) summary

PRK09103
Location:4 → 761

PRK09103; ribonucleoside-diphosphate reductase subunit alpha