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nrdD anaerobic ribonucleoside-triphosphate reductase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948755, updated on 30-Jul-2025
Official Symbol
nrdD
Official Full Name
anaerobic ribonucleoside-triphosphate reductase
Primary source
ECOCYC:EG11417
Locus tag
b4238
See related
ASAP:ABE-0013865
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
ECK4233
Summary
Activated NrdD is predicted to be cleaved by oxygen at the Gly681 radical, dropping the last 31 aa. [More information is available at EcoGene: EG11417]. The NrdD reductase is activated by the NrdG activase under anaerobic conditions and is inactivated by oxygen. [More information is available at EcoCyc: EG11417].
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Sequence:
NC_000913.3 (4460522..4462660, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene pseudo Neighboring gene anaerobic ribonucleoside-triphosphate reductase activating protein Neighboring gene trehalose-6-phosphate hydrolase Neighboring gene trehalose-specific PTS enzyme IIBC component

Genomic Sequence:
NC_000913.3
Products Interactant Other Gene Complex Source Pubs Description

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
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 dATP binding IDA
Inferred from Direct Assay
more info
PubMed 
enables dGTP binding IDA
Inferred from Direct Assay
more info
PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
 
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 pyrimidine deoxyribonucleotide binding IDA
Inferred from Direct Assay
more info
PubMed 
contributes_to 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 IMP
Inferred from Mutant Phenotype
more info
PubMed 
enables ribonucleoside-triphosphate reductase (thioredoxin) activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables ribonucleoside-triphosphate reductase (thioredoxin) activity IDA
Inferred from Direct Assay
more info
PubMed 
enables ribonucleoside-triphosphate reductase (thioredoxin) activity IEA
Inferred from Electronic Annotation
more info
 
enables zinc ion binding IDA
Inferred from Direct Assay
more info
PubMed 
Component Evidence Code Pubs
part_of anaerobic ribonucleoside-triphosphate reductase complex IBA
Inferred from Biological aspect of Ancestor
more info
 
part_of anaerobic ribonucleoside-triphosphate reductase complex IDA
Inferred from Direct Assay
more info
PubMed 
part_of anaerobic ribonucleoside-triphosphate reductase complex IMP
Inferred from Mutant Phenotype
more info
PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 
Preferred Names
anaerobic ribonucleoside-triphosphate reductase
NP_418659.1

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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
    4460522..4462660 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418659.1 anaerobic ribonucleoside-triphosphate reductase

    See identical proteins and their annotated locations for NP_418659.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A3R0NDP9, A0A5B9AQK8
    Conserved Domains (1) summary
    PRK09263
    Location:1711
    PRK09263; anaerobic ribonucleoside triphosphate reductase; Provisional