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CinA family protein
CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation [1]. This Pfam family consists of putative competence-damaged proteins from the cin operon. Some members of this family have nicotinamide mononucleotide (NMN) deamidase activity [2]. [1]. 7538190. The recA gene of Streptococcus pneumoniae is part of a competence-induced operon and controls lysogenic induction. Martin B, Garcia P, Castanie MP, Claverys JP;. Mol Microbiol 1995;15:367-379. [2]. 21953451. Identification of nicotinamide mononucleotide deamidase of the bacterial pyridine nucleotide cycle reveals a novel broadly conserved amidohydrolase family. Galeazzi L, Bocci P, Amici A, Brunetti L, Ruggieri S, Romine M, Reed S, Osterman AL, Rodionov DA, Sorci L, Raffaelli N;. J Biol Chem. 2011;286:40365-40375. (from Pfam)
competence/damage-inducible CinA family protein containing only the C-terminal CinA domain, similar to Pseudomonas putida nicotinamide-nucleotide (NMN) amidohydrolase PncC
nicotinamide-nucleotide amidohydrolase family protein
The nicotinamide-nucleotide amidohydrolase domain family contains active enzymes and apparently inactive homologs as well. Member proteins in the family contain both extended forms with an additional fused ADP-ribose pyrophosphatase or a NUDIX hydrolase activity (MocF) domain. PMID:28388636 (2017) recommends using CinA for proteins consisting only of a functional nicotinamide-nucleotide amidohydrolase domain, and using PncC for the longer, fused forms. Note that E. coli encodes a paralog of the CinA/PncC enzyme, called YdeJ, that appears inactive and whose role and function are unknown.
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