Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic Gene Ontology annotation based on Rhea mapping
The anaerobic ribonucleotide reductase from Escherichia coli. The small protein is an activating enzyme containing a [4fe-4s](2+) center.
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NrdG carries one [4Fe-4S] centre per polypeptide and acts catalytically, activating several NrdD molecules.
"protein beta has the potential to activate several molecules of protein alpha, suggesting that protein beta is an activating enzyme rather than a component of an alpha(2)beta(2) complex as previously claimed"
The activating component of the anaerobic ribonucleotide reductase from Escherichia coli. An iron-sulfur center with only three cysteines.
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Three cysteines of the CxxxCxxC motif ligate the [4Fe-4S] cluster, and NrdG transfers electrons from reduced flavodoxin to SAM.
"By site-directed mutagenesis we demonstrate that the three cysteines of the conserved CXXXCXXC sequence are involved in iron chelation."
Characterization of components of the anaerobic ribonucleotide reductase system from Escherichia coli.
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The anaerobic system is a ribonucleoside triphosphate reductase in which dA3 (NrdD) is the reductase and dA1 (NrdG) is auxiliary.
"dA3 is the actual ribonucleoside triphosphate reductase; dA1 has an auxiliary function."
Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins.
The binary protein-protein interaction landscape of Escherichia coli.
Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme.
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The nrdG ORF downstream of nrdD encodes an iron-containing activase that is required for NrdD glycyl radical formation and binds the reductase tightly.
"The protein corresponding to this open reading frame is required for the generation of the glycyl radical of the anaerobic reductase and binds tightly to the reductase."
An iron-sulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli.
The anaerobic Escherichia coli ribonucleotide reductase. Subunit structure and iron sulfur center.
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NrdG carries the 4Fe-4S cluster and forms a tight 1:1 complex with NrdD, whose glycyl radical is at Gly681.
"The large and the small proteins form a tight complex."
nrdD and nrdG genes are essential for strict anaerobic growth of Escherichia coli.
Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction.
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NrdG binds SAM (Kd 10 uM) and its Fe-S centre reductively cleaves it, forming methionine and the NrdD glycyl radical.
"Here, we demonstrate that AdoMet is directly reduced by the Fe-S center of beta2 during the activation of the enzyme, resulting in methionine and glycyl radical formation."
UniProt entry P0A9N8 (NRDG_ECOLI)