3.1.13.3: oligonucleotidase
This is an abbreviated version!
For detailed information about oligonucleotidase, go to the full flat file.
Word Map on EC 3.1.13.3
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3.1.13.3
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exoribonuclease
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exonuclease
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trna
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oligoribonucleotides
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pnpase
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cyclic-di-gmp
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exonucleolytic
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phosphoesterase
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c-di-gmp
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deddh
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3'-phosphoadenosine
- 3.1.13.3
- exoribonuclease
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exonuclease
- trna
- oligoribonucleotides
- pnpase
- cyclic-di-gmp
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exonucleolytic
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phosphoesterase
- c-di-gmp
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deddh
- 3'-phosphoadenosine
Reaction
exonucleolytic cleavage of oligonucleotides to yield nucleoside 5'-phosphates =
Synonyms
CpsORN, EC 3.1.4.19, More, nanoRNase, NrnC, nucleotidase, oligo-, oligoribonuclease, ORN, phosphodiesterase, REXO2, RNase T, small fragment nuclease, XC847, YtqI
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General Information on EC 3.1.13.3 - oligonucleotidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
evolution
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Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
malfunction
mutation of gene orn leads to the accumulation of pGpG, which inhibits the function of glutamate-alanine-leucine (EAL) domain-containing enzymes, resulting in increased levels of cyclic-di-GMP and the consequent hyperbiofilm phenotype. EAL domain-containing enzymes hydrolyze cyclic-di-GMP to 5'-phosphoguanylyl-(3',5')-guanosine (pGpG). Mutation of orn drastically increases bacterial susceptibility to quinolones but not to tetracycline, aminoglycoside, or beta-lactam antibiotics. Upregulation of pyocin genes contributes to increased susceptibility to ciprofloxacin in the orn mutant. PrtR stability is reduced by the mutation of orn. Expression levels of prtN and PA0613 in wild-type and DELTAorn mutant strains PA14, phenotypes, overview
malfunction
Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
malfunction
the lysates from DELTAorn show 25fold decrease in 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) hydrolysis. Complementation with wild-type, but not active site mutants, restores hydrolysis. Accumulation of pGpG in the DELTAorn strain inhibits PDE-As, increasing cyclic-diguanylate (c-di-GMP) concentration. Increased transcription from the cyclic-diguanylate-regulated pel promoter is observed. Additionally, the cyclic-diguanylate-governed auto-aggregation and biofilm phenotypes are elevated in the DELTAorn strain in a pel-dependent manner. Detection of elevated levels of pGpG and cyclic-diguanylate in the DELTAorn strain. Phenotype, overview
malfunction
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Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
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malfunction
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Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
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malfunction
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Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
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malfunction
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Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
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malfunction
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Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
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malfunction
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Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
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malfunction
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Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
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physiological function
depletion of isoform REXO2 by RNA interference causes a strong morphological phenotype in human cells, which show a disorganized network of punctate and granular mitochondria. Lack of REXO2 protein also causes a substantial decrease of mitochondrial nucleic acid content and impaires de novo mitochondrial protein synthesis
physiological function
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expression of isoform NrnC in Escherichia coli can complement lack of oligoribonuclease Orn. Knock down of NrnC decreases the growth ability of Bartonella henselae
physiological function
bacterial oligoribonuclease (Orn) is a conserved 3'-to-5' exonuclease. In Pseudomonas aeruginosa, Orn plays a major role in the hydrolysis of pGpG, which is required for cyclic-di-GMP homeostasis. Orn is involved in the degradation of nanoRNAs, which can alter global gene expression by serving as transcription initiation primers. And Orn is required for the type III secretion system and pathogenesis of Pseudomonas aeruginosa, indicating a role of Orn in the bacterial response to environmental stimuli. Orn is required for the tolerance of Pseudomonas aeruginosa to ciprofloxacin, role of Orn in bacterial resistance to antibiotics. And role of Orn in genome integrity and bacterial resistance to quinolones. Oligoribonuclease is required for bacterial resistance to fluoroquinolones
physiological function
cells regulate their intracellular mRNA levels by using specific ribonucleases. Oligoribonuclease (ORN) is a 3'-5' exoribonuclease for small RNA molecules, important in RNA degradation and re-utilisation
physiological function
oligoribonuclease (Orn), an exoribonuclease that hydrolyzes two- to five-nucleotide-long RNAs, is the primary enzyme responsible for degrading 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) in cells. Orn binds to pGpG specifically and can cleave it into GMP. pGpG inhibits RocR phosphodiesterase activity by binding to the active site and competing for cyclic diguanylate binding in the active site, and excess pGpG extends cyclic diguanylate half-life in vitro
physiological function
oligoribonuclease (Orn), which had earlier been established as an essential enzyme in most bacteria involved in the recycling of RNA into ribonucleotides, acts as c-di-GMP PDB-B in Pseudomonas aeruginosa cleaving diguanylate into (pGpG), and pGpG then into GMP
physiological function
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
physiological function
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the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
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physiological function
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the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
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physiological function
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the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
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physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
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physiological function
Colwellia psychrerythraea ATCC BAA-681
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cells regulate their intracellular mRNA levels by using specific ribonucleases. Oligoribonuclease (ORN) is a 3'-5' exoribonuclease for small RNA molecules, important in RNA degradation and re-utilisation
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additional information
structure analysis, identification of active site structure and key residues responsible for enzymatic catalysis of CpsORN, the active site of CpsORN has a negatively charged surface, created by Asp12, Glu14, Asp112, and Asp163, overview. His66 is located near the active site and potentially stabilises the negative charge of the nucleotide. His66 residue also plays a significant role in the cleavage mechanism. His66 and His158 are completely conserved among other ORNs. Residues Ser108 and Tyr129 are not essential for the RNase activity of CpsORN
additional information
Colwellia psychrerythraea ATCC BAA-681
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structure analysis, identification of active site structure and key residues responsible for enzymatic catalysis of CpsORN, the active site of CpsORN has a negatively charged surface, created by Asp12, Glu14, Asp112, and Asp163, overview. His66 is located near the active site and potentially stabilises the negative charge of the nucleotide. His66 residue also plays a significant role in the cleavage mechanism. His66 and His158 are completely conserved among other ORNs. Residues Ser108 and Tyr129 are not essential for the RNase activity of CpsORN
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