Information on EC 5.4.99.42 - tRNA pseudouridine31 synthase

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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

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EC NUMBER
COMMENTARY hide
5.4.99.42
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RECOMMENDED NAME
GeneOntology No.
tRNA pseudouridine31 synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tRNA uridine31 = tRNA pseudouridine31
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
tRNA-uridine31 uracil mutase
The enzyme specifically acts on uridine31 in tRNA.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the deletion mutant strain DELTAYGR169c shows no detectable growth phenotype. The only difference in pseudouridine formation in stable cellular RNAs is the absence of pseudouridine at position 31 in cytoplasmic and mitochondrial tRNAs. Complementation of the DELTAYGR169c strain by a plasmid bearing the wild-type YGR169c ORF restores pseudouridine31 formation in tRNA
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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
tRNA uridine31
tRNA pseudouridine31
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
tRNA uridine31
tRNA pseudouridine31
show the reaction diagram
P53294
the enzyme is responsible for modification of cytoplasmic and mitochondrial tRNAs at position 31
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged Ygr169 protein produced in Escherichia coli is capable of forming pseudouridine31 in vitro using tRNAs extracted from the DELTAYGR169c yeast cells as substrates
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ENGINEERING
ORGANISM
UNIPROT
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LITERATURE
D168A
mutation abolishes tRNA pseudouridine31 synthase activity
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LINKS TO OTHER DATABASES (specific for EC-Number 5.4.99.42)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)