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nitroreductase family protein
The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds. [1]. 8846223. Crystal structure of NADH oxidase from Thermus thermophilus. Hecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD. Nat Struct Biol 1995;2:1109-1114. [2]. 17331467. In silico identification of a new group of specific bacterial and fungal nitroreductases-like proteins. de Oliveira IM, Henriques JA, Bonatto D;. Biochem Biophys Res Commun. 2007;355:919-925. (from Pfam)
SagB/ThcOx family dehydrogenase
SagB/ThcOx family dehydrogenase such as Escherichia coli microcin B17-processing protein McbC that is necessary to process the inactive microcin B17 (McbA) precursor into the active peptide
SagB family peptide dehydrogenase
SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. The cyanobactin oxidase ThcOx likewise participates in peptide modification for form a natural product. TIGR03605 describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603) and SgaD-like (see TIGR03604) proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases.
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