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Literature summary for 4.1.99.22 extracted from
- The role of SufS is restricted to Fe-S cluster biosynthesis in Escherichia coli (2017), Biochemistry, 56, 1987-2000 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | deletion of central components of the ISC system in addition to IscS leads to an overall decrease in Fe-S cluster enzyme and molybdoenzyme activity in addition to a decrease in the number of Fe-S-dependent thiomodifications of tRNA, based on the fact that some proteins involved in Moco biosynthesis and tRNA thiolation are Fe-S-dependent. Complementation of the ISC deficient strains with the suf operon restores the activity of Fe-S-containing proteins, including the MoaA protein, which is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate in the fist step of Moco biosynthesis | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Escherichia coli BW25113 | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MoaA | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme MoaA catalyzes the fist step of molybdenum cofactor (Moco) biosynthesis | Escherichia coli |
| physiological function | the MoaA protein is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate in the fist step of molybdenum cofactor (Moco) biosynthesis | Escherichia coli |
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