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5'-nucleotidase C-terminal domain-containing protein
metallophosphoesterase
This family includes a diverse range of phosphoesterases [1], including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD Swiss:P13457 or yeast MRE11 Swiss:P32829. The most conserved regions in this superfamily centre around the metal chelating residues. [1]. 9685491. Phosphoesterase domains associated with DNA polymerases of diverse origins. Aravind L, Koonin EV;. Nucleic Acids Res 1998;26:3746-3752. (from Pfam)
2',3'-cyclic-nucleotide 2'-phosphodiesterase
2',3'-cyclic-nucleotide 2'-phosphodiesterase is a bifunctional enzyme localized to the periplasm of Gram-negative bacteria. 2',3'-cyclic-nucleotide 2'-phosphodiesters are intermediates formed during the hydrolysis of RNA by the ribonuclease I, which is also found to the periplasm, and other enzymes of the RNAse T2 family. Bacteria are unable to transport 2',3'-cyclic-nucleotides into the cytoplasm. 2',3'-cyclic-nucleotide 2'-phosphodiesterase contains 2 active sites which catalyze the reactions that convert the 2',3'-cyclic-nucleotide into a 3'-nucleotide, which is then converted into nucleic acid and phosphate. Both final products can be transported into the cytoplasm. Thus, it has been suggested that 2',3'-cyclic-nucleotide 2'-phosphodiesterase has a 'scavenging' function. Experimental evidence indicates that 2',3'-cyclic-nucleotide 2'-phosphodiesterase enables Yersinia enterocolitica O:8 to grow on 2'3'-cAMP as a sole source of carbon and energy (PMID:11160814).
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase catalyzes the phosphodiester hydrolysis of 2',3'-cyclic nucleotides to 2'-nucleotides
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
Functions during ribonucleic acid degradation; 2',3'-cyclic nucleotides are first converted to 3'-nucleotide and then cleaved to yield a ribonucleotide and a phosphate
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