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Information on EC 6.1.1.5 - isoleucine-tRNA ligase and Organism(s) Bacillus subtilis and UniProt Accession Q45477

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Bacillus subtilis
UNIPROT: Q45477 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
isoleucyl-trna synthetase, ilers, iars2, isoleucyl trna synthetase, iles2, ile-trna synthetase, isoleucine-trna synthetase, mitochondrial isoleucyl-trna synthetase, iles1, isoleucyl-transfer rna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Isoleucyl-tRNA synthetase
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IleRS
IRS
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-
-
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Isoleucine translase
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-
-
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Isoleucine--tRNA ligase
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-
-
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Isoleucine-transfer RNA ligase
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-
-
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Isoleucine-tRNA synthetase
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-
-
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Isoleucyl-transfer ribonucleate synthetase
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-
-
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Isoleucyl-transfer RNA synthetase
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-
-
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Isoleucyl-tRNA synthetase
Mupirocin resistance protein
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-
-
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Synthetase, isoleucyl-transfer ribonucleate
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
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esterification
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-
-
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aminacylation
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-
-
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deacylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-isoleucine:tRNAIle ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-96-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine, the lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by IleRS
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-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine, the lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by IleRS
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
activity assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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mutant ileS(T233P) allows tRNAIle mischarging while retaining wild-type Ile-tRNAIle synthesis activity. The growth rate of the ileS(T233P) strain BAL4571 is not significantly different from wild-type strain BAL4574. The ileS(T233P) strain is observed to exhibit a significant defect in formation of environmentally resistant spores. The sporulation defect ranges from 3fold to 30fold and is due to a delay in activation of early sporulation genes. The loss of aminoacylation quality control in the ileS(T233P) strain results in the inability to compete with a wild-type strain under selective conditions that require sporulation. The quality control-defective IleRS mutant is defective in expressing genes activated by the master regulator of sporulation, Spo0A. Phenotype, overview. Spo0A is the first transcription factor to become active, through phosphorylation by a phosphorelay, in the sporulation regulatory cascade
physiological function
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isoleucyl-tRNA synthetase (IleRS) is an aminoacyl-tRNA synthetase whose essential function is to aminoacylate tRNAIle with isoleucine. Like some other aminoacyl-tRNA synthetases, IleRS can mischarge tRNAIle and correct this misacylation through a separate post-transfer editing function, biological significance of this editing function. The quality control function of IleRS is required in Bacillus subtilis for efficient sporulation and editing by aminoacyl-tRNA synthetases may be important for survival under starvation/nutrient limitation conditions. Isoleucine-tRNA synthetase (IleRS) possesses quality control functions that discriminate between isoleucine, the non-cognate amino acid valine, and the non-proteinogenic amino acids, norvaline, a by-product of branched-chain amino acid synthesis, and homocysteine (Hcy), a by-product from degradation of S-adenosylhomocysteine by LuxS in bacteria
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T233P
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site-directed mutagenesis, mutant ileS(T233P) allows tRNAIle mischarging while retaining wild-type Ile-tRNAIle synthesis activity. The growth rate of the ileS(T233P)strain is not significantly different from wild-type. The ileS(T233P) strain is observed to exhibit a significant defect in formation of environmentally resistant spores. The sporulation defect ranges from 3fold to 30fold and is due to a delay in activation of early sporulation genes. The loss of aminoacylation quality control in the ileS(T233P) strain results in the inability to compete with a wild-type strain under selective conditions that require sporulation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using M2-FLAG resin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the vector pET3D-FLAG for expression in Escherichia coli BL21DE3 cells
subcloning and expression of wild-type and mutant enzymes in Escherichia coli Top10 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Salowe, S.P.; Wiltsie, J.; Hawkins, J.C.; Sonatore, L.M.
The catalytic flexibility of tRNAIle-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase
J. Biol. Chem.
284
9656-9662
2009
Bacillus subtilis (Q45477), Bacillus subtilis, Bacillus subtilis 168 (Q45477)
Manually annotated by BRENDA team
Kermgard, E.; Yang, Z.; Michel, A.M.; Simari, R.; Wong, J.; Ibba, M.; Lazazzera, B.A.
Quality control by isoleucyl-tRNA synthetase of Bacillus subtilis is required for efficient sporulation
Sci. Rep.
7
41763
2017
Bacillus subtilis, Bacillus subtilis BAL4574
Manually annotated by BRENDA team