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Information on EC 6.3.4.22 - tRNAIle2-agmatinylcytidine synthase
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6.3.4.22 tRNAIle2-agmatinylcytidine synthaseIUBMB Comments
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 .
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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+
+
=
[tRNAIle2]-2-agmatinylcytidine34
+
+
2
Synonyms
AF2259, TiaS, tRNAIle-2-agmatinylcytidine synthetase, tRNAIle-agm2C synthetase, tRNAIle-agmatidine synthetase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AF2259
TiaS
tRNAIle-2-agmatinylcytidine synthetase
tRNAIle-agm2C synthetase
tRNAIle-agmatidine synthetase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + agmatine + [tRNAIle2]-cytidine34 + H2O = [tRNAIle2]-2-agmatinylcytidine34 + AMP + 2 phosphate
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SYSTEMATIC NAME
IUBMB Comments
agmatine:[tRNAIle]-cytidine34 ligase
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 .
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + ?
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-
-
?
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + ?
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-
-
?
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
the enzyme catalyzes the essential modification at the anticodon wobble position (position 34) of the AUA-codon of tRNAIle
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-
?
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
the precursor form of tRNAIle bearing an unmodified cytidine at the wobble position (C34) is aminoacylated with methionine (Met) and decodes the AUG codon.The Thr18-Cyt34 kinase domain first hydrolyzes ATP into AMP and diphosphate, then phosphorylates the C2 position of cytidine34 with the gamma-phosphate. Next, the amino group of agmatine attacks this position to release the phosphate and form 2-agmatinylcytidine. The Thr18-Cyt34 kinase domain also autophosphorylates the Thr18 of the enzyme, which may be involved in 2-agmatinylcytidine formation. Catalytic efficiency (kcat/Km) with GTP, UTP or CTP as substrate is less than 1% compared to ATP
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + ?
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-
-
?
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
the enzyme catalyzes the essential modification at the anticodon wobble position (position 34) of the AUA-codon of tRNAIle
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00037
alpha,beta-methyleneadenosine 5'-triphosphate
Archaeoglobus fulgidus
pH 8.8, 70°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
modification at the anticodon wobble position of archaeal tRNAIle2. According to the chemical structure of agm2C, conjugation of an agmatine moiety at the C2 position of cytosine induces a tautomeric conversion with protonation of the N3 position and imino group formation at the C4 position. This modification completely alters the proton donor-acceptor pattern of cytosine in Watson-Click hydrogen bonding to that of uracil, enabling agm2C to base pair with adenine instead of guanine. tRNAIle2 acquires the ability to decode the AUA codon via formation 2-agmatinylcytidine
physiological function
modification at the anticodon wobble position of archaeal tRNAIle2. According to the chemical structure of agm2C, conjugation of an agmatine moiety at the C2 position of cytosine induces a tautomeric conversion with protonation of the N3 position and imino group formation at the C4 position. This modification completely alters the proton donor-acceptor pattern of cytosine in Watson-Click hydrogen bonding to that of uracil, enabling agm2C to base pair with adenine instead of guanine. tRNAIle2 acquires the ability to decode the AUA codon via formation 2-agmatinylcytidine
Show AA Sequence and Transmembrane Helices (1563 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
the Thr18-Cyt34 kinase domain autophosphorylates the Thr18 of the enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the enzyme-tRNAIle complexed with ATP, or with alpha,beta-methyleneadenosine 5'-triphosphate and agmatine
the enzyme is cocrystallized with both tRNAIle2 and ATP by the vapour-diffusion method. The crystals of the TiaSâtRNAIle2âATP complex diffract to 2.9 A resolution. The crystals belong to the hexagonal space group P3(2)21, with unit-cell parameters a = b = 131.1, c = 86.6 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R217A
C352A/C355A
almost no 2-agmatinylcytidine formation is observed
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ikeuchi, Y.; Kimura, S.; Numata, T.; Nakamura, D.; Yokogawa, T.; Ogata, T.; Wada, T.; Suzuki, T.; Suzuki, T.
Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea
Nat. Chem. Biol.
6
277-282
2010
Archaeoglobus fulgidus (O28025), Pyrococcus horikoshii (O59476)
brenda
Osawa, T.; Inanaga, H.; Kimura, S.; Terasaka, N.; Suzuki, T.; Numata, T.
Crystallization and preliminary X-ray diffraction analysis of an archaeal tRNA-modification enzyme, TiaS, complexed with tRNA(Ile2) and ATP
Acta Crystallogr. Sect. F
67
1414-1416
2011
Archaeoglobus fulgidus (O28025)
brenda
Terasaka, N.; Kimura, S.; Osawa, T.; Numata, T.; Suzuki, T.
Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS
Nat. Struct. Mol. Biol.
18
1268-1274
2011
Archaeoglobus fulgidus (O28025)
brenda
Osawa, T.; Kimura, S.; Terasaka, N.; Inanaga, H.; Suzuki, T.; Numata, T.
Structural basis of tRNA agmatinylation essential for AUA codon decoding
Nat. Struct. Mol. Biol.
18
1275-1280
2011
Archaeoglobus fulgidus (O28025)
brenda
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