Entry
Name
tRNAIle2-agmatinylcytidine synthase;
TiaS;
AF2259;
tRNAIle-2-agmatinylcytidine synthetase;
tRNAIle-agm2C synthetase;
tRNAIle-agmatidine synthetase
Class
Ligases;
Forming carbon-nitrogen bonds;
Other carbon-nitrogen ligases
BRITE hierarchy
Sysname
agmatine:[tRNAIle]-cytidine34 ligase
Reaction(IUBMB)
ATP + agmatine + [tRNAIle2]-cytidine34 + H2O = [tRNAIle2]-2-agmatinylcytidine34 + AMP + 2 phosphate [RN:
R10496 ]
Reaction(KEGG)
Substrate
Product
[tRNAIle2]-2-agmatinylcytidine34;
AMP [CPD:
C00020 ];
phosphate [CPD:
C00009 ]
Comment
The enzyme from the archaeon Archaeoglobus fulgidus modifies the wobble base of the CAU anticodon of the archaeal tRNAIle2 at the oxo group in position 2 of cytidine34. This modification is crucial for accurate decoding of the genetic code. In bacteria EC
6.3.4.19 , tRNAIle-lysidine synthase, catalyses the modification of [tRNAIle2]-cytidine34 to [tRNAIle2]-lysidine34 .
History
EC 6.3.4.22 created 2013
Orthology
K06932 tRNA(Ile2)-agmatinylcytidine synthase
Genes
HJT : DVR14_16035 DVR14_20155
TVO : TVG0590669(TVG0590669)
BARC : AOA65_1257(tiaS_1) AOA65_1587(tiaS_2)
» show all
Taxonomy
Reference
Authors
Ikeuchi Y, Kimura S, Numata T, Nakamura D, Yokogawa T, Ogata T, Wada T, Suzuki T, Suzuki T
Title
Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea.
Journal
Sequence
Reference
Authors
Terasaka N, Kimura S, Osawa T, Numata T, Suzuki T
Title
Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS.
Journal
Reference
Authors
Osawa T, Inanaga H, Kimura S, Terasaka N, Suzuki T, Numata T
Title
Crystallization and preliminary X-ray diffraction analysis of an archaeal tRNA-modification enzyme, TiaS, complexed with tRNA(Ile2) and ATP.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 6.3.4.22
ExPASy - ENZYME nomenclature database: 6.3.4.22
LinkDB
All DBs