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Literature summary extracted from

  • Buehning, M.; Valleriani, A.; Leimkuehler, S.
    The role of SufS is restricted to Fe-S cluster biosynthesis in Escherichia coli (2017), Biochemistry, 56, 1987-2000 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.22 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

EC Number Organism UniProt Comment Textmining
4.1.99.22 Escherichia coli
-
-
-
4.1.99.22 Escherichia coli BW25113
-
-
-

Synonyms

EC Number Synonyms Comment Organism
4.1.99.22 MoaA
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
4.1.99.22 metabolism the enzyme MoaA catalyzes the fist step of molybdenum cofactor (Moco) biosynthesis Escherichia coli
4.1.99.22 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