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Information on EC 4.6.1.22 - Bacillus subtilis ribonuclease and Organism(s) Thermus thermophilus and UniProt Accession Q72JJ7

for references in articles please use BRENDA:EC4.6.1.22
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EC Tree
IUBMB Comments
This enzyme catalyses endonucleolytic cleavage to 2',3'-cyclic nucleotides. The cyclic products may be hydrolysed to the corresponding 3'-phosphates by 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16). The enzyme from B. subtilis is inhibited by ATP.
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q72JJ7
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Word Map
The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
=
a 5'-hydroxy-ribonucleotide
+
n
nucleoside-2',3'-cyclophosphates
Synonyms
rnase y, rnase j, rnase j1, rnase j2, bacillus subtilis ribonuclease, ribonuclease p protein, endoribonuclease rnase y, ribonuclease rnase j1, bacisubin, endoribonuclease j2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bifunctional 5'-3' exo/endoribonuclease
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intracellular acid ribonuclease
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-
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Proteus mirabilis RNase-2
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-
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ribonucleate nucleotido-2'-transferase (cyclizing)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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SYSTEMATIC NAME
IUBMB Comments
[RNA] 5'-hydroxy-ribonucleotide-3'-[RNA fragment]-lyase (cyclicizing; [RNA fragment]-3'- nucleoside -2',3'-cyclophosphate-forming)
This enzyme catalyses endonucleolytic cleavage to 2',3'-cyclic nucleotides. The cyclic products may be hydrolysed to the corresponding 3'-phosphates by 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16). The enzyme from B. subtilis is inhibited by ATP.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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RNase J is a bifunctional 5'-3' exo/endoribonuclease, structure of enzyme bound to a 4-nucleotide RNA showing an RNA-binding channel. A second, negatively charged tunnel leads from the active site, and is ideally located to evacuate the cleaved nucleotide in 5'-3' exonucleolytic mode
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
binding structure in the beta-lactamase domain of the enzyme, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
RNase J is a key member of the beta-CASP family of metallo-beta-lactamases
physiological function
enzyme RNase J has been shown to play an extensive role in mRNA turnover. The bifunctional 5'-3' exo/endoribonuclease RNase J is involved in the maturation and turnover of RNAs in prokaryotes
additional information
modeling of the enzyme reaction involving the binding of the RNA to the surface of the beta-CASP domain to explain the enzyme's processive action, enzyme residues involved in RNA recognition, RNA-binding channel and proposed nucleotide Exit tunnel of RNase J, modeling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme with bound 4 nt RNA with sequence CUGG or a 16 nt RNA, using catalytically inactive mutant H77A and a 2'-O-methylated, 3'-fluorescein-labeled RNAs, X-ray diffraction crystal structure determination and analysis at 2.5-3.1 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H77A
catalytically inactive mutant
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dorleans, A.; Li de la Sierra-Gallay, I.; Piton, J.; Zig, L.; Gilet, L.; Putzer, H.; Condon, C.
Molecular basis for the recognition and cleavage of RNA by the bifunctional 5'-3' exo/endoribonuclease RNase J
Structure
19
1252-1261
2011
Bacillus subtilis, Thermus thermophilus (Q72JJ7)
Manually annotated by BRENDA team