EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.17.4.1 | C428S | mutantion is lethal. Cells carrying both the C428S and the SX2S mutation of CX2C motif on plasmids are viable and form colonies with an efficiency similar to that of the wild-type control showing interallelic complementation | Saccharomyces cerevisiae |
1.17.4.1 | C439S | the C439S mutant of the Escherichia coli R1 is catalytically inactive in vitro | Escherichia coli |
1.17.4.1 | additional information | deletion of C-terminal domain of subunit R1 is lethal. Mutation of CX2C motif to SX2S results in viable, but slowly growing cells. Mutant cells exhibit a prolonged S phase | Saccharomyces cerevisiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.17.4.1 | Sml1 | inhibitor protein Sml1 competes with the C-terminal domain of subunit R1 for association with its N-terminal domain to hinder the accessibility of the CX2C motif to the active site for R1 regeneration during the catalytic cycle | Saccharomyces cerevisiae | |
1.17.4.1 | Sml1 protein | a 104-residue Saccharomyces cerevisiae protein, inhibits ribonucleotide reductase activity by binding to the R1 subunit interacting with the N-terminal domain of R1, R1-NTD, which involves a conserved two-residue sequence motif in the R1-NTD, the Sml1-R1 interaction causes SML1-dependent lethality, overview | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.17.4.1 | nucleus | - |
Escherichia coli | 5634 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.4.1 | additional information | Escherichia coli | the Sml1-R1 interaction causes SML1-dependent lethality, the CX2C motif of Rnr1 Is essential for viability. overview | ? | - |
? | |
1.17.4.1 | ribonucleoside 5'-diphosphate + thioredoxin | Escherichia coli | - |
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.17.4.1 | Escherichia coli | - |
- |
- |
1.17.4.1 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.4.1 | additional information | the Sml1-R1 interaction causes SML1-dependent lethality, the CX2C motif of Rnr1 Is essential for viability. overview | Escherichia coli | ? | - |
? | |
1.17.4.1 | ribonucleoside 5'-diphosphate + thioredoxin | - |
Escherichia coli | 2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O | - |
? | |
1.17.4.1 | ribonucleoside 5'-diphosphate + thioredoxin | at the completion of each turnover cycle, the active site of R1 becomes oxidized and subsequently regenerates by a cysteine pair at its C-terminal domain R1-CTD, that acts in trans to reduce the active site of its neighboring monomer, R1-CTD interacts with the N-terminal domain of R1, R1-NTD, which involves a conserved two-residue sequence motif in the R1-NTD, overview | Escherichia coli | 2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.17.4.1 | More | C-terminal domain of subunit R1 acts in trans to reduce the active site of its neighbouring monomer and interacts with the N-terminal domain of neighbouring R1. Inhibitor protein Sml1 competes with the C-terminal domain of R1 for association with the N-terminal domain to hinder the accessibility of the CX2C motif to the active site for R1 regeneration during the catalytic cycle | Saccharomyces cerevisiae |
1.17.4.1 | More | 2 * R1 subunit + 2 * R2 subunit, cross-talk Between the C-terminus of one subunit R1 monomer and the active site of its neighboring monomer, overview | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.17.4.1 | ribonucleotide reductase | - |
Escherichia coli |
1.17.4.1 | RNR | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.17.4.1 | thioredoxin | - |
Escherichia coli |