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Information on EC 1.14.11.42 - tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase and Organism(s) Homo sapiens and UniProt Accession A2RUC4

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IUBMB Comments
Requires Fe2+. The enzyme is not active with wybutosine.
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This record set is specific for:
Homo sapiens
UNIPROT: A2RUC4
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
tRNA wybutosine-synthesizing protein 5, tRNA yW-synthesizing enzyme 5, TYW5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tRNA wybutosine-synthesizing protein 5
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tRNA yW-synthesizing enzyme 5
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TYW5
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SYSTEMATIC NAME
IUBMB Comments
tRNAPhe 7-(3-amino-3-carboxypropyl)wyosine37,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Requires Fe2+. The enzyme is not active with wybutosine.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7-(3-amino-3-carboxypropyl)wyosine37 in tRNAPhe + 2-oxoglutarate + O2
7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe + succinate + CO2
show the reaction diagram
enzyme catalyzes the hydroxylation of the hypermodified nucleoside wybutoside in position 37 of tRNAPhe. Residues Y106 and L175 are required for 2-oxoglutarate binding. H160, N162, and H235 are residues in the HX(D/E)XnH motif that are required for Fe(II) binding
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additional information
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in the biogenesis of hydroxywybutosine, enzyme Tyw5p employs wybutosine residue 72 in tRNAPhe as a substrate by recognizing the N4-methyl group to hydroxylate the beta-carbon of the propyl group, followed by methylation and methoxycarbonylation of the side chain catalyzed by enzyme Tyw4 for completion
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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
7-(3-amino-3-carboxypropyl)wyosine37 in tRNAPhe + 2-oxoglutarate + O2
7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe + succinate + CO2
show the reaction diagram
enzyme catalyzes the hydroxylation of the hypermodified nucleoside wybutoside in position 37 of tRNAPhe. Residues Y106 and L175 are required for 2-oxoglutarate binding. H160, N162, and H235 are residues in the HX(D/E)XnH motif that are required for Fe(II) binding
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
residues H160, N162, and H235 in the HX(D/E)XnH motif are required for Fe(II) binding
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
knock-down of enzyme gene by RNAi results in loss of hydroxywybutosine. Expression of the gene in yeast leads to formation of hydroxywybutosine. Enzyme Tyw5p employs wybutosine residue 72 in tRNAPhe as a substrate by recognizing the N4-methyl group to hydroxylate the beta-carbon of the propyl group, followed by methylation and methoxycarbonylation of the side chain catalyzed by enzyme Tyw4 for completion
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TYW5_HUMAN
315
0
36548
Swiss-Prot
other Location (Reliability: 4)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the free and complex forms with 2-oxoglutarate and Ni(II) ion at 2.5 and 2.8 A resolution, respectively. The catalytic domain consists of a beta-jellyroll fold. The enzyme forms a homodimer through C-terminal helix bundle formation, thereby presenting a large, positively charged patch involved in tRNA binding. In a docking model of the TYW5-tRNAPhe complex, the D arm is captured by the positively charged patch, and the anticodon loop is directed into the positively charged catalytic pocket
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noma, A.; Ishitani, R.; Kato, M.; Nagao, A.; Nureki, O.; Suzuki, T.
Expanding role of the jumonji C domain as an RNA hydroxylase
J. Biol. Chem.
285
34503-34507
2010
Homo sapiens (A2RUC4)
Manually annotated by BRENDA team
Kato, M.; Araiso, Y.; Noma, A.; Nagao, A.; Suzuki, T.; Ishitani, R.; Nureki, O.
Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification
Nucleic Acids Res.
39
1576-1585
2011
Homo sapiens (A2RUC4)
Manually annotated by BRENDA team