NP_416737.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
Molecular Weight
101.8 kDa
NCBI Official Full Name
ribonucleoside-diphosphate reductase 1, alpha subunit
NCBI Protein Information
ribonucleoside-diphosphate reductase 1, alpha subunit
UniProt Protein Name
Ribonucleoside-diphosphate reductase 1 subunit alpha
UniProt Synonym Protein Names
Protein B1; Ribonucleoside-diphosphate reductase 1 R1 subunit; Ribonucleotide reductase 1
UniProt Synonym Gene Names
UniProt Entry Name
RIR1_ECOLI
NCBI Summary for nrdA
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].
UniProt Comments for nrdA
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines.
Product References and Citations for nrdA recombinant protein
Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon.Carlson J., Fuchs J.A., Messing J.Proc. Natl. Acad. Sci. U.S.A. 81:4294-4297(1984)
Nucleotide sequence of the gene coding for the large subunit of ribonucleotide reductase of Escherichia coli. Correction.Nilsson O., Aaberg A., Lundqvist T., Sjoeberg B.-M.Nucleic Acids Res. 16:4174-4174(1988)
Sjoeberg B.-M.Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.DNA Res. 4:91-113(1997)
The complete genome sequence of Escherichia coli K-12.Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.Science 277:1453-1462(1997)
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.Mol. Syst. Biol. 2:E1-E5(2006)
Protein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotide sequence of the Escherichia coli nrdA gene.Sjoeberg B.-M., Eriksson S., Joernvall H., Carlquist M., Eklund H.Eur. J. Biochem. 150:423-427(1985)
Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli.Aaberg A., Hahne S., Karlsson M., Larsson A., Ormoe M., Aahgren A., Sjoeberg B.-M.J. Biol. Chem. 264:12249-12252(1989)
Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase.Ekberg M., Sahlin M., Eriksson M., Sjoberg B.M.J. Biol. Chem. 271:20655-20659(1996)
Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.Mol. Cell. Proteomics 8:215-225(2009)
Structure of ribonucleotide reductase protein R1.Uhlin U., Eklund H.Nature 370:533-539(1994)
A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase.Persson A.L., Eriksson M., Katterle B., Potsch S., Sahlin M., Sjoberg B.M.J. Biol. Chem. 272:31533-31541(1997)
Binding of allosteric effectors to ribonucleotide reductase protein R1
reduction of active-site cysteines promotes substrate binding.Eriksson M., Uhlin U., Ramaswamy S., Ekberg M., Regnstroem K., Sjoeberg B.-M., Eklund H.Structure 5:1077-1092(1997)
Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction.Berardi M.J., Bushweller J.H.J. Mol. Biol. 292:151-161(1999)
Research Articles on nrdA
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Products associated with nrdA recombinant protein
Pathways associated with nrdA recombinant protein
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