EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.72 | protein Hfq | the multifunctional protein Hfq, originally discovered as a host factor for phage Qb, can stimulate the CCA-adding activity, Hfq facilitates the release of the reaction product, after CCA addition has taken place | Thermus thermophilus | |
2.7.7.72 | protein Hfq | the multifunctional protein Hfq, originally discovered as a host factor for phage Qb, can stimulate the CCA-adding activity, Hfq facilitates the release of the reaction product, after CCA addition has taken place | Escherichia coli | |
2.7.7.72 | protein Hfq | the multifunctional protein Hfq, originally discovered as a host factor for phage Qb, can stimulate the CCA-adding activity, Hfq facilitates the release of the reaction product, after CCA addition has taken place | Homo sapiens | |
2.7.7.72 | protein Hfq | the multifunctional protein Hfq, originally discovered as a host factor for phage Qb, can stimulate the CCA-adding activity, Hfq facilitates the release of the reaction product, after CCA addition has taken place | Geobacillus stearothermophilus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.7.7.72 | crystal structure analysis | Escherichia coli |
2.7.7.72 | crystal structure analysis | Archaeoglobus fulgidus |
2.7.7.72 | crystal structure analysis | Thermotoga maritima |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.72 | Mg2+ | two metal ions are bound to the two catalytically important carboxylates. The first metal ion deprotonates the 3'-OH group of the tRNA primer and activates the resulting 3'-O for an attack at the a-phosphate of the incoming nucleotide. The second metal ion stabilizes the triphosphate moiety of the NTP and facilitates the leaving of the pyrophosphate group, overview | Archaeoglobus fulgidus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.72 | additional information | Thermus thermophilus | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | ? | - |
? | |
2.7.7.72 | additional information | Escherichia coli | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | ? | - |
? | |
2.7.7.72 | additional information | Homo sapiens | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | ? | - |
? | |
2.7.7.72 | additional information | Geobacillus stearothermophilus | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | ? | - |
? | |
2.7.7.72 | additional information | Saccharolobus shibatae | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | ? | - |
? | |
2.7.7.72 | additional information | Archaeoglobus fulgidus | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | ? | - |
? | |
2.7.7.72 | additional information | Thermotoga maritima | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.72 | Archaeoglobus fulgidus | - |
- |
- |
2.7.7.72 | Escherichia coli | - |
- |
- |
2.7.7.72 | Geobacillus stearothermophilus | - |
- |
- |
2.7.7.72 | Homo sapiens | - |
- |
- |
2.7.7.72 | Saccharolobus shibatae | - |
- |
- |
2.7.7.72 | Thermotoga maritima | - |
- |
- |
2.7.7.72 | Thermus thermophilus | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.7.7.72 | a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate | catalytic core and reaction mechanism of class I CCA-adding enzymes, overview | Saccharolobus shibatae | |
2.7.7.72 | a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate | catalytic core and reaction mechanism of class I CCA-adding enzymes, overview | Archaeoglobus fulgidus | |
2.7.7.72 | a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate | catalytic core and reaction mechanism of class II CCA-adding enzymes, overview | Thermus thermophilus | |
2.7.7.72 | a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate | catalytic core and reaction mechanism of class II CCA-adding enzymes, overview | Homo sapiens | |
2.7.7.72 | a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate | catalytic core and reaction mechanism of class II CCA-adding enzymes, overview | Geobacillus stearothermophilus | |
2.7.7.72 | a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate | catalytic core and reaction mechanism of class II CCA-adding enzymes, overview | Thermotoga maritima |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.72 | additional information | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | Thermus thermophilus | ? | - |
? | |
2.7.7.72 | additional information | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | Escherichia coli | ? | - |
? | |
2.7.7.72 | additional information | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | Homo sapiens | ? | - |
? | |
2.7.7.72 | additional information | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | Geobacillus stearothermophilus | ? | - |
? | |
2.7.7.72 | additional information | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | Saccharolobus shibatae | ? | - |
? | |
2.7.7.72 | additional information | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | Archaeoglobus fulgidus | ? | - |
? | |
2.7.7.72 | additional information | CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview | Thermotoga maritima | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.7.72 | CCA-adding enzyme | - |
Thermus thermophilus |
2.7.7.72 | CCA-adding enzyme | - |
Escherichia coli |
2.7.7.72 | CCA-adding enzyme | - |
Homo sapiens |
2.7.7.72 | CCA-adding enzyme | - |
Geobacillus stearothermophilus |
2.7.7.72 | CCA-adding enzyme | - |
Saccharolobus shibatae |
2.7.7.72 | CCA-adding enzyme | - |
Archaeoglobus fulgidus |
2.7.7.72 | CCA-adding enzyme | - |
Thermotoga maritima |
2.7.7.72 | class I CCA-adding enzyme | - |
Saccharolobus shibatae |
2.7.7.72 | class I CCA-adding enzyme | - |
Archaeoglobus fulgidus |
2.7.7.72 | class II CCA-adding enzyme | - |
Thermus thermophilus |
2.7.7.72 | class II CCA-adding enzyme | - |
Homo sapiens |
2.7.7.72 | class II CCA-adding enzyme | - |
Geobacillus stearothermophilus |
2.7.7.72 | class II CCA-adding enzyme | - |
Thermotoga maritima |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.7.72 | evolution | a class I CCA-adding enzyme. CCA-adding enzymes are essential RNA polymerases that emerged twice in evolution leading to different structural characteristics and unusual mechanistic solutions for an error-free and sequence-specific CCA polymerization reaction. The catalytic cleft is formed by the head, neck, and body domains. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview | Saccharolobus shibatae |
2.7.7.72 | evolution | a class I CCA-adding enzyme. CCA-adding enzymes are essential RNA polymerases that emerged twice in evolution leading to different structural characteristics and unusual mechanistic solutions for an error-free and sequence-specific CCA polymerization reaction. The catalytic cleft is formed by the head, neck, and body domains. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview | Archaeoglobus fulgidus |
2.7.7.72 | evolution | a class II CCA-adding enzyme. Compared to class I, class II CCA-adding enzymes show a much higher evolutionary conservation of individual catalytic core motifs. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview | Thermus thermophilus |
2.7.7.72 | evolution | a class II CCA-adding enzyme. Compared to class I, class II CCA-adding enzymes show a much higher evolutionary conservation of individual catalytic core motifs. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview | Homo sapiens |
2.7.7.72 | evolution | a class II CCA-adding enzyme. Compared to class I, class II CCA-adding enzymes show a much higher evolutionary conservation of individual catalytic core motifs. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview | Geobacillus stearothermophilus |
2.7.7.72 | evolution | a class II CCA-adding enzyme. Compared to class I, class II CCA-adding enzymes show a much higher evolutionary conservation of individual catalytic core motifs. The templating motif carries the sequence DDxxR, a slight deviation from the usual EDxxR motif. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview | Thermotoga maritima |
2.7.7.72 | evolution | CCA-adding enzymes are essential RNA polymerases that emerged twice in evolution leading to different structural characteristics and unusual mechanistic solutions for an error-free and sequence-specific CCA polymerization reaction. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview | Escherichia coli |
2.7.7.72 | malfunction | mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding | Thermus thermophilus |
2.7.7.72 | malfunction | mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding | Homo sapiens |
2.7.7.72 | malfunction | mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding | Geobacillus stearothermophilus |
2.7.7.72 | malfunction | mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding | Saccharolobus shibatae |
2.7.7.72 | malfunction | mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding | Thermotoga maritima |
2.7.7.72 | malfunction | the enzyme knockout phenotype is a dramatic growth impairment, indicating the repair function of the CCA-adding enzyme on defective tRNAs lacking CCA ends due to hydrolytic damage | Escherichia coli |
2.7.7.72 | additional information | structure-function relationship, overview | Escherichia coli |
2.7.7.72 | additional information | structure-function relationship, overview | Saccharolobus shibatae |
2.7.7.72 | additional information | structure-function relationship, overview. The active site is located in the N-terminal part of the enzyme and consists of five elements that are involved in metal ion binding, catalysis, ribose recognition, nucleotide selection, and templating. Motif A is located in the head domain and includes the general signature motif of all nucleotidyltransferases with the two metal-binding carboxylates DxD that are involved in catalysis and binding of the triphosphate moiety of the incoming nucleotides. The head domain carries motif B, where highly conserved residues play a critical role in discriminating between NTPs and dNTPs. The neck domain contains motif D, a single nucleotide-binding pocket that is specific for binding of CTP and ATP. Head and neck domain form a cleft that binds the incoming nucleotide as well as the 3'-end of the tRNA primer. The body and tail domains at the enzyme's C-terminus recognize the top-half region of the tRNA primer. The CCA-enzyme does not move along the tRNA during synthesis but remains at a fixed position | Thermus thermophilus |
2.7.7.72 | additional information | structure-function relationship, overview. The active site is located in the N-terminal part of the enzyme and consists of five elements that are involved in metal ion binding, catalysis, ribose recognition, nucleotide selection, and templating. Motif A is located in the head domain and includes the general signature motif of all nucleotidyltransferases with the two metal-binding carboxylates DxD that are involved in catalysis and binding of the triphosphate moiety of the incoming nucleotides. The head domain carries motif B, where highly conserved residues play a critical role in discriminating between NTPs and dNTPs. The neck domain contains motif D, a single nucleotide-binding pocket that is specific for binding of CTP and ATP. Head and neck domain form a cleft that binds the incoming nucleotide as well as the 3'-end of the tRNA primer. The body and tail domains at the enzyme's C-terminus recognize the top-half region of the tRNA primer. The CCA-enzyme does not move along the tRNA during synthesis but remains at a fixed position | Homo sapiens |
2.7.7.72 | additional information | structure-function relationship, overview. The active site is located in the N-terminal part of the enzyme and consists of five elements that are involved in metal ion binding, catalysis, ribose recognition, nucleotide selection, and templating. Motif A is located in the head domain and includes the general signature motif of all nucleotidyltransferases with the two metal-binding carboxylates DxD that are involved in catalysis and binding of the triphosphate moiety of the incoming nucleotides. The head domain carries motif B, where highly conserved residues play a critical role in discriminating between NTPs and dNTPs. The neck domain contains motif D, a single nucleotide-binding pocket that is specific for binding of CTP and ATP. Head and neck domain form a cleft that binds the incoming nucleotide as well as the 3'-end of the tRNA primer. The body and tail domains at the enzyme's C-terminus recognize the top-half region of the tRNA primer. The CCA-enzyme does not move along the tRNA during synthesis but remains at a fixed position | Geobacillus stearothermophilus |
2.7.7.72 | additional information | structure-function relationship, overview. The active site is located in the N-terminal part of the enzyme and consists of five elements that are involved in metal ion binding, catalysis, ribose recognition, nucleotide selection, and templating. Motif A is located in the head domain and includes the general signature motif of all nucleotidyltransferases with the two metal-binding carboxylates DxD that are involved in catalysis and binding of the triphosphate moiety of the incoming nucleotides. The head domain carries motif B, where highly conserved residues play a critical role in discriminating between NTPs and dNTPs. The neck domain contains motif D, a single nucleotide-binding pocket that is specific for binding of CTP and ATP. Head and neck domain form a cleft that binds the incoming nucleotide as well as the 3'-end of the tRNA primer. The body and tail domains at the enzyme's C-terminus recognize the top-half region of the tRNA primer. The CCA-enzyme does not move along the tRNA during synthesis but remains at a fixed position | Thermotoga maritima |
2.7.7.72 | additional information | structure-function relationship, overview. The enzyme binds the tRNA top half in the correct orientation for CCA-addition in a cleft, the tRNA acceptor stem interacts with a highly conserved long alpha-helical element in an almost parallel orientation. In the position of nucleotide addition, the 3'-end is bound to the active site located in the enzyme's head domain, while the T loop of the tRNA contacts the tail domain. The bound tRNA substrate remains fixed at its binding site in the enzyme during the complete nucleotide incorporation process | Archaeoglobus fulgidus |
2.7.7.72 | physiological function | CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Second, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms | Archaeoglobus fulgidus |
2.7.7.72 | physiological function | CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Second, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms, but in Escherichia coli, on the other hand, where CCA ends are encoded, this enzyme is dispensable, and a corresponding gene knockout is not lethal, but the repair function of the CCA-adding enzyme on defective tRNAs lacking CCA ends due to hydrolytic damage is required | Escherichia coli |
2.7.7.72 | physiological function | CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms | Thermus thermophilus |
2.7.7.72 | physiological function | CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms | Homo sapiens |
2.7.7.72 | physiological function | CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms | Geobacillus stearothermophilus |
2.7.7.72 | physiological function | CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms | Saccharolobus shibatae |
2.7.7.72 | physiological function | CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms | Thermotoga maritima |