Entry |
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Name |
RNA 3'-terminal-phosphate cyclase (ATP);
rtcA (gene name);
RNA cyclase (ambiguous);
RNA-3'-phosphate cyclase (ambiguous)
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Class |
Ligases;
Forming phosphoric-ester bonds;
Ligases that form phosphoric-ester bonds (only sub-subclass identified to date)
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Sysname |
RNA-3'-phosphate:RNA ligase (cyclizing, AMP-forming)
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Reaction(IUBMB) |
ATP + [RNA]-3'-(3'-phospho-ribonucleoside) = AMP + diphosphate + [RNA]-3'-(2',3'-cyclophospho)-ribonucleoside (overall reaction) [RN: R04274];
(1a) ATP + [RNA 3'-phosphate cyclase]-L-histidine = [RNA 3'-phosphate cyclase]-Ntau-(5'-adenylyl)-L-histidine + diphosphate;
(1b) [RNA 3'-phosphate cyclase]-Ntau-(5'-adenylyl)-L-histidine + [RNA]-3'-(3'-phospho-ribonucleoside) = [RNA 3'-phosphate cyclase]-L-histidine + [RNA]-3'-ribonucleoside-3'-(5'-diphosphoadenosine);
(1c) [RNA]-3'-ribonucleoside-3'-(5'-diphosphoadenosine) = [RNA]-3'-(2',3'-cyclophospho)-ribonucleoside + AMP
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Reaction(KEGG) |
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Substrate |
ATP [CPD: C00002];
[RNA]-3'-(3'-phospho-ribonucleoside);
[RNA 3'-phosphate cyclase]-L-histidine;
[RNA 3'-phosphate cyclase]-Ntau-(5'-adenylyl)-L-histidine;
[RNA]-3'-ribonucleoside-3'-(5'-diphosphoadenosine)
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Product |
AMP [CPD: C00020];
diphosphate [CPD: C00013];
[RNA]-3'-(2',3'-cyclophospho)-ribonucleoside;
[RNA 3'-phosphate cyclase]-Ntau-(5'-adenylyl)-L-histidine;
[RNA 3'-phosphate cyclase]-L-histidine;
[RNA]-3'-ribonucleoside-3'-(5'-diphosphoadenosine)
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Comment |
The enzyme converts the 3'-terminal phosphate of various RNA substrates into the 2',3'-cyclic phosphodiester in an ATP-dependent reaction. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a histidine residue [5,6]. The adenylate group is then transferred to the 3'-phosphate terminus of the substrate, forming the capped structure [RNA]-3'-(5'-diphosphoadenosine). Finally, the enzyme catalyses an attack of the vicinal O-2' on the 3'-phosphorus, which results in formation of cyclic phosphate and release of the adenylate. The enzyme also has a polynucleotide 5' adenylylation activity [7]. cf. EC 6.5.1.5, RNA 3'-terminal-phosphate cyclase (GTP).
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History |
EC 6.5.1.4 created 1986, modified 1989, modified 2013, modified 2016
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Orthology |
K01974 | RNA 3'-terminal phosphate cyclase (ATP) |
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Genes |
» show all
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Reference |
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Authors |
Filipowicz W, Konarska M, Gross HJ, Shatkin AJ. |
Title |
RNA 3'-terminal phosphate cyclase activity and RNA ligation in HeLa cell extract. |
Journal |
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Reference |
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Authors |
Reinberg D, Arenas J, Hurwitz J. |
Title |
The enzymatic conversion of 3'-phosphate terminated RNA chains to 2',3'-cyclic phosphate derivatives. |
Journal |
J Biol Chem 260:6088-97 (1985) |
Reference |
|
Authors |
Genschik P, Billy E, Swianiewicz M, Filipowicz W |
Title |
The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea. |
Journal |
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Reference |
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Authors |
Genschik P, Drabikowski K, Filipowicz W |
Title |
Characterization of the Escherichia coli RNA 3'-terminal phosphate cyclase and its sigma54-regulated operon. |
Journal |
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Reference |
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Authors |
Billy E, Hess D, Hofsteenge J, Filipowicz W |
Title |
Characterization of the adenylation site in the RNA 3'-terminal phosphate cyclase from Escherichia coli. |
Journal |
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Reference |
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Authors |
Tanaka N, Shuman S |
Title |
Structure-activity relationships in human RNA 3'-phosphate cyclase. |
Journal |
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Reference |
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Authors |
Chakravarty AK, Shuman S |
Title |
RNA 3'-phosphate cyclase (RtcA) catalyzes ligase-like adenylylation of DNA and RNA 5'-monophosphate ends. |
Journal |
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Reference |
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Authors |
Das U, Shuman S |
Title |
2'-Phosphate cyclase activity of RtcA: a potential rationale for the operon organization of RtcA with an RNA repair ligase RtcB in Escherichia coli and other bacterial taxa. |
Journal |
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Other DBs |
ExplorEnz - The Enzyme Database: | 6.5.1.4 |
ExPASy - ENZYME nomenclature database: | 6.5.1.4 |
BRENDA, the Enzyme Database: | 6.5.1.4 |
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LinkDB |
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