Literature summary extracted from

Dantuluri, S.; Abdullahu, L.; Munir, A.; Katolik, A.; Damha, M.J.; Shuman, S.
Substrate analogs that trap the 2'-phospho-ADP-ribosylated RNA intermediate of the Tpt1 (tRNA 2'-phosphotransferase) reaction pathway (2020), RNA, 26, 373-381 .

Inhibitors

EC Number	Inhibitors	Comment	Organism
2.7.1.160	2'-fluoroarabinose	replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2'' nucleophile) results in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. High utilization of ara-2''F-NAD+ as a substrate by Clostridium thermocellum Tpt1 does indeed results in trapping of the step 1 reaction product	Acetivibrio thermocellus
2.7.1.160	2'-fluoroarabinose	replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2'' nucleophile) results in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. High utilization of ara-2''F-NAD+ as a substrate by Runella slithyformis Tpt1 does indeed results in trapping of the step 1 reaction product	Runella slithyformis
2.7.1.160	2'-fluoroarabinose	replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2''-nucleophile) results in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. Low to moderate utilization of ara-2''F-NAD+ as a substrate by Chaetomium thermophilum Tpt1 results in partial trapping of the step 1 reaction product	Thermochaetoides thermophila
2.7.1.160	ara-2''F-NAD+	human Tpt1 effects no detectable reaction of the 2'-phosphate RNA substrate in the presence of 0.05 mM ara-2''F-NAD+	Homo sapiens
2.7.1.160	ara-2''F-NAD+	Chaetomium Tpt1 forms the dead-end product in the presence of 0.05 mM ara-2''F-NAD+, though the extent of substrate conversion is low	Thermochaetoides thermophila
2.7.1.160	arabinose-2'-phosphate	replacement of the RNA ribose-2'-phosphate nucleotide with arabinose-2'-phosphate selectively slows step 2 of the reaction pathway and results in the transient accumulation of high levels of the reaction intermediate	Acetivibrio thermocellus
2.7.1.160	arabinose-2'-phosphate	replacement of the RNA ribose-2'-phosphate nucleotide with arabinose-2'-phosphate selectively slows step 2 of the reaction pathway and results in the transient accumulation of high levels of the reaction intermediate	Runella slithyformis
2.7.1.160	arabinose-2'-phosphate	replacement of the RNA ribose-2'-phosphate nucleotide with arabinose-2'-phosphate selectively slows step 2 of the reaction pathway and results in the transient accumulation of high levels of the reaction intermediate	Thermochaetoides thermophila
2.7.1.160	additional information	analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes	Acetivibrio thermocellus
2.7.1.160	additional information	analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes, reveals that replacement of the RNA ribose-2'-phosphate nucleotide with arabinose-2'-phosphate selectively slows step 2 of the reaction pathway and results in the transient accumulation of high levels of the reaction intermediate. Replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2''-nucleophile) results in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. Replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2''-nucleophile) can result in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. But no utilization of ara-2''F-NAD+ or arabinose-2'-phosphate as substrates by human Tpt1 is detected	Homo sapiens
2.7.1.160	additional information	analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes	Runella slithyformis
2.7.1.160	additional information	analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes	Thermochaetoides thermophila
2.7.1.160	PS-2'-FANA oligonucleotides	phosphorothioate (PS) modifications of the 3'-5' phosphodiester backbone of DNA and 2'-FANA oligonucleotides (PS-DNA and PS-2'-FANA oligos) give substrates that are completely converted to 2'-hydroxy products by RslTpt1. Runella Tpt1 specific activity is reduced by 11fold and 7fold, respectively, by the PS modifications of DNA and 2'-FANA substrates	Runella slithyformis
2.7.1.160	PS-DNA oligonucleotides	phosphorothioate (PS) modifications of the 3'-5'-phosphodiester backbone of DNA and 2'-FANA oligonucleotides (PS-DNA and PS-2'-FANA oligos) give substrates that are completely converted to 2'-hydroxy products by RslTpt1. Runella Tpt1 specific activity is reduced by 11fold and 7fold, respectively, by the PS modifications of DNA and 2'-FANA substrates	Runella slithyformis

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Homo sapiens	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Runella slithyformis	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Acetivibrio thermocellus	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Thermochaetoides thermophila	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Thermochaetoides thermophila IMI 039719	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Acetivibrio thermocellus DSM 1237	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Thermochaetoides thermophila DSM 1495	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Acetivibrio thermocellus JCM 9322	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Acetivibrio thermocellus NBRC 103400	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Acetivibrio thermocellus ATCC 27405	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Acetivibrio thermocellus VPI 7372	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Thermochaetoides thermophila CBS 144.50	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Acetivibrio thermocellus NCIMB 10682	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	Acetivibrio thermocellus NRRL B-4536	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.1.160	Acetivibrio thermocellus	A3DJX6	Clostridium thermocellum	-
2.7.1.160	Acetivibrio thermocellus ATCC 27405	A3DJX6	Clostridium thermocellum	-
2.7.1.160	Acetivibrio thermocellus DSM 1237	A3DJX6	Clostridium thermocellum	-
2.7.1.160	Acetivibrio thermocellus JCM 9322	A3DJX6	Clostridium thermocellum	-
2.7.1.160	Acetivibrio thermocellus NBRC 103400	A3DJX6	Clostridium thermocellum	-
2.7.1.160	Acetivibrio thermocellus NCIMB 10682	A3DJX6	Clostridium thermocellum	-
2.7.1.160	Acetivibrio thermocellus NRRL B-4536	A3DJX6	Clostridium thermocellum	-
2.7.1.160	Acetivibrio thermocellus VPI 7372	A3DJX6	Clostridium thermocellum	-
2.7.1.160	Homo sapiens	Q86TN4	-	-
2.7.1.160	Runella slithyformis	-	-	-
2.7.1.160	Thermochaetoides thermophila	G0S5Z5	-	-
2.7.1.160	Thermochaetoides thermophila CBS 144.50	G0S5Z5	-	-
2.7.1.160	Thermochaetoides thermophila DSM 1495	G0S5Z5	-	-
2.7.1.160	Thermochaetoides thermophila IMI 039719	G0S5Z5	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Homo sapiens	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Runella slithyformis	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Acetivibrio thermocellus	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Thermochaetoides thermophila	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Thermochaetoides thermophila IMI 039719	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Acetivibrio thermocellus DSM 1237	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Thermochaetoides thermophila DSM 1495	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Acetivibrio thermocellus JCM 9322	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Acetivibrio thermocellus NBRC 103400	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Acetivibrio thermocellus ATCC 27405	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Acetivibrio thermocellus VPI 7372	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Thermochaetoides thermophila CBS 144.50	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Acetivibrio thermocellus NCIMB 10682	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	2'-phospho-[ligated tRNA] + NAD+	-	Acetivibrio thermocellus NRRL B-4536	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Thermochaetoides thermophila	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances. Runella Tpt1 (RslTpt1) efficiently removes an internal 2'-phosphate from a DNA substrate. RslTpt1 removes the 2'-phosphate from the 2'-fluoroarabinonucleic acid (2'-FANA) substrate, albeit with about 7fold lower specific activity compared to the 6mer 2'-phosphate RNA control substrate. The 2'-phospho-ADP-ribosylated intermediate accumulates to an extent of 4% of total labeled RNA at low enzyme concentrations. Phosphorothioate (PS) modifications of the 3'-5'-phosphodiester backbone of DNA and 2'-FANA oligonucleotides (PS-DNA and PS-2'-FANA oligos) give substrates that are completely converted to 2'-hydroxy products by RslTpt1 but with reduced activity	Runella slithyformis	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2''- to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Homo sapiens	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Acetivibrio thermocellus	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Thermochaetoides thermophila IMI 039719	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Acetivibrio thermocellus DSM 1237	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Thermochaetoides thermophila DSM 1495	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Acetivibrio thermocellus JCM 9322	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Acetivibrio thermocellus NBRC 103400	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Acetivibrio thermocellus ATCC 27405	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Acetivibrio thermocellus VPI 7372	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Thermochaetoides thermophila CBS 144.50	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Acetivibrio thermocellus NCIMB 10682	?	-	-
2.7.1.160	additional information	the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances	Acetivibrio thermocellus NRRL B-4536	?	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
2.7.1.160	Tpt1	-	Homo sapiens
2.7.1.160	Tpt1	-	Runella slithyformis
2.7.1.160	Tpt1	-	Acetivibrio thermocellus
2.7.1.160	Tpt1	-	Thermochaetoides thermophila
2.7.1.160	tRNA 2'-phosphotransferase	-	Homo sapiens
2.7.1.160	tRNA 2'-phosphotransferase	-	Runella slithyformis
2.7.1.160	tRNA 2'-phosphotransferase	-	Acetivibrio thermocellus
2.7.1.160	tRNA 2'-phosphotransferase	-	Thermochaetoides thermophila

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.7.1.160	37	-	assay at	Homo sapiens
2.7.1.160	37	-	assay at	Runella slithyformis
2.7.1.160	37	-	assay at	Acetivibrio thermocellus
2.7.1.160	37	-	assay at	Thermochaetoides thermophila

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
2.7.1.160	7.5	-	assay at	Homo sapiens
2.7.1.160	7.5	-	assay at	Runella slithyformis
2.7.1.160	7.5	-	assay at	Acetivibrio thermocellus
2.7.1.160	7.5	-	assay at	Thermochaetoides thermophila

Cofactor

EC Number	Cofactor	Comment	Organism
2.7.1.160	NAD+	-	Homo sapiens
2.7.1.160	NAD+	-	Runella slithyformis
2.7.1.160	NAD+	-	Acetivibrio thermocellus
2.7.1.160	NAD+	-	Thermochaetoides thermophila

General Information

EC Number	General Information	Comment	Organism
2.7.1.160	malfunction	inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop	Homo sapiens
2.7.1.160	malfunction	inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop	Runella slithyformis
2.7.1.160	malfunction	inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop	Acetivibrio thermocellus
2.7.1.160	malfunction	inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop	Thermochaetoides thermophila
2.7.1.160	additional information	Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologs catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2'- or 3'-terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction	Homo sapiens
2.7.1.160	additional information	Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction	Thermochaetoides thermophila
2.7.1.160	additional information	Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism	Acetivibrio thermocellus
2.7.1.160	additional information	Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Runella slithyformis Tpt1 has a Arg-His-Arg-Arg catalytic tetrad in the active site	Runella slithyformis
2.7.1.160	physiological function	tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate	Runella slithyformis
2.7.1.160	physiological function	tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate	Acetivibrio thermocellus
2.7.1.160	physiological function	tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2''- to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate	Thermochaetoides thermophila
2.7.1.160	physiological function	tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate; and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate	Homo sapiens