Information on EC 6.3.4.22 - tRNAIle2-agmatinylcytidine synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.3.4.22
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RECOMMENDED NAME
GeneOntology No.
tRNAIle2-agmatinylcytidine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + agmatine + [tRNAIle2]-cytidine34 + H2O = [tRNAIle2]-2-agmatinylcytidine34 + AMP + 2 phosphate
show the reaction diagram
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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 .
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + ?
show the reaction diagram
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + ?
show the reaction diagram
O28025
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ATP + agmatine + [tRNAIle2]-cytidine34
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
show the reaction diagram
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the enzyme catalyzes the essential modification at the anticodon wobble position (position 34) of the AUA-codon of tRNAIle
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
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optimal concentration: 100 mM
Mg2+
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optimal concentration: 2-5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha,beta-methyleneadenosine 5'-triphosphate
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beta,gamma-methyleneadenosine 5'-triphosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00087
agmatine
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pH 8.8, 70°C
0.006
ATP
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pH 8.8, 70°C
0.00029
[tRNAIle2]-cytidine34
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pH 8.8, 70°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
agmatine
Archaeoglobus fulgidus
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pH 8.8, 70°C
0.0062
ATP
Archaeoglobus fulgidus
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pH 8.8, 70°C
0.0065
[tRNAIle2]-cytidine34
Archaeoglobus fulgidus
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pH 8.8, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.9
agmatine
Archaeoglobus fulgidus
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pH 8.8, 70°C
505
1
ATP
Archaeoglobus fulgidus
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pH 8.8, 70°C
4
22.41
[tRNAIle2]-cytidine34
Archaeoglobus fulgidus
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pH 8.8, 70°C
3948
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00037
alpha,beta-methyleneadenosine 5'-triphosphate
Archaeoglobus fulgidus
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pH 8.8, 70°C
0.00079
beta,gamma-methyleneadenosine 5'-triphosphate
Archaeoglobus fulgidus
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pH 8.8, 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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the Thr18-Cyt34 kinase domain autophosphorylates the Thr18 of the enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of the enzyme-tRNAIle complexed with ATP, or with alpha,beta-methyleneadenosine 5'-triphosphate and agmatine
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the enzyme is cocrystallized with both tRNAIle2 and ATP by the vapour-diffusion method. The crystals of the TiaS–tRNAIle2–ATP 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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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overexpressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C17A
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complete loss of activity
C17S
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complete loss of activity
C210S
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complete loss of activity
C352A/C355A
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almost no 2-agmatinylcytidine formation is observed
D11A
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complete loss of activity
D8A
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complete loss of activity
D9A
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complete loss of activity
E159A
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complete loss of activity
F286A
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complete loss of activity
F301A
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complete loss of activity
G218A
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mutation reduces activity
I143A
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reduced activity
I49A
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reduced activity
K52A
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complete loss of activity
N194A
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reduced activity
N56A
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complete loss of activity
R140/G141A
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mutation completely abolishes activity
R164A
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mutation reduces activity
R369A
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complete loss of activity
R44A
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complete loss of activity
R54A
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complete loss of activity
T18A
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complete loss of activity
T18D
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complete loss of activity
T248A/D249A
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mutation reduces activity
T53A
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complete loss of activity
Y163A
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mutation reduces activity
Show AA Sequence (485 entries)
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