Information on EC 2.7.7.B5 - adenylyltransferase ThiI

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.7.B5
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
adenylyltransferase ThiI
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tRNA-uridine + ATP = adenylated-trNA-uridine + diphosphate
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + TPHE39A
adenylated TPHE39A + diphosphate
show the reaction diagram
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truncated tRNA consisting of 39 nucleotides derived from tRNAPhe, minimal RNA substrate for modification by ThiI. The crystal structure of TPHE39A shows that base pairs in the T-stem are almost completely disrupted, although those in the acceptor-stem are preserved. ThiI can efficiently bind with not only tRNAPhe but also TPHE39A
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-
?
tRNA-uridine + ATP
adenylated-trNA-uridine + diphosphate
show the reaction diagram
tRNA-uridine + GTP
adenylated-trNA-uridine + diphosphate
show the reaction diagram
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kcat/Km for GTP is about 6fold lower than the value for ATP
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-
?
additional information
?
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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
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24
ATP
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pH 7.5, 22°C
0.84
GTP
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pH 7.5, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.604
ATP
Escherichia coli
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pH 7.5, 22°C
0.113
GTP
Escherichia coli
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pH 7.5, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
THiI-RNA complex
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
MBP-fusion protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D189A
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mutation eliminates in vivo function of the enzyme
K321M
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mutation eliminates in vivo function of the enzyme
C207S
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using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis but not for thiazole synthesis
C344S
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using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis but not for thiazole synthesis
C456S
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using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis and for thiazole synthesis
D189A
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using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis but not for thiazole synthesis
K321M
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using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis but not for thiazole synthesis
additional information
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construction of two truncated forms of ThiI containing the N-terminal domain including NFLD and THUMP, and the C-terminal domain including the PP-loop and RLD domains, respectively. The N-domain can bind with both tRNAPhe and TPHE39A and recognizes the acceptor-stem region, whereas the C-domain cannot. The C-domain also affects RNA binding by its enthalpically favorable, but entropically unfavorable, contribution. The C-domain induces a conformation change in tRNAPhe