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

Gene ID: 946612, updated on 26-Mar-2025
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].
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Sequence:
NC_000913.3 (2344865..2347150)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative autotransporter adhesin YfaL Neighboring gene protein YpaB Neighboring gene protein YoaM Neighboring gene ribonucleoside-diphosphate reductase 1 subunit beta Neighboring gene ferredoxin-like diferric-tyrosyl radical cofactor maintenance protein YfaE

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Protein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotide sequence of the Escherichia coli nrdA gene. Sjöberg BM, et al. Eur J Biochem, 1985 Aug 1. PMID 3894026
  2. SOS system induction in Escherichia coli cells with distinct levels of ribonucleotide reductase activity. Villaverde A, et al. Mutat Res, 1992 Feb. PMID 1370982
  3. REP sequences: Mediators of the environmental stress response? Liang W, et al. RNA Biol, 2016. PMID 26574793, Free PMC Article
  4. Identification of an active site residue of the R1 subunit of ribonucleotide reductase from Escherichia coli: characterization of substrate-induced polypeptide cleavage by C225SR1. van der Donk WA, et al. Biochemistry, 1996 Aug 6. PMID 8756468
  5. Turning on ribonucleotide reductase by light-initiated amino acid radical generation. Chang MC, et al. Proc Natl Acad Sci U S A, 2004 May 4. PMID 15123822, Free PMC Article

See all (115) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. 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.
  2. 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.
  3. 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?
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
  9. 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.
  10. 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)
Products Interactant Other Gene Complex Source Pubs Description

Homology

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 catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
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 
enables ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor IBA
Inferred from Biological aspect of Ancestor
more info
  
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 
Preferred Names
ribonucleoside-diphosphate reductase 1 subunit alpha
NP_416737.1

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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
    2344865..2347150
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. 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
Nucleotide Protein
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