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Information on EC 2.9.1.3 - tRNA 2-selenouridine synthase
for references in articles please use BRENDA:EC2.9.1.3
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EC Tree 2 Transferases
2.9 Transferring selenium-containing groups
2.9.1 Selenotransferases
2.9.1.3 tRNA 2-selenouridine synthase
IUBMB Comments
This bacterial enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA. The enzyme contains a rhodanese domain.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
show+
+
+
=
+
+
+
+
+
5-methylaminomethyl-2-thiouridine34 in tRNA
+
=
5-methylaminomethyl-2-selenouridine34 in tRNA
+
(2E)-3,7-dimethylocta-2,6-diene-1-thiol
+
+
Synonyms
trna 2-selenouridine synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
mnmH
-
-
-
-
selU
sufY
-
-
-
-
tRNA 2-selenouridine synthase
-
ybbB
selU
-
-
-
-
ybbB
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + H2O = 5-methylaminomethyl-2-selenouridine34 in tRNA + phosphate
(1c)
-
-
-
geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA = 5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA + diphosphate
(1a)
-
-
-
selenophosphate + 5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA = 5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol
(1b)
-
-
-
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O = 5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
overall reaction
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
geranyl diphosphate/selenophosphate:tRNA 5-methylaminomethyl-2-thiouridine34 geranyl/selenophosphatetransferase
This bacterial enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA. The enzyme contains a rhodanese domain.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + phosphate
geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA
5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA + diphosphate
selenophosphate + 5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + phosphate
Substrates: -
Products: -
Products: -
?
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + phosphate
Substrates: -
Products: -
Products: -
?
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + phosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA
5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA
5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA
5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA + diphosphate
Substrates: -
Products: -
Products: -
?
selenophosphate + 5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol
Substrates: -
Products: -
Products: -
?
selenophosphate + 5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol
Substrates: -
Products: -
Products: -
?
selenophosphate + 5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: the enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: overall reaction. Reaction with tRNA anticodon-stem-loop fragments. The enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA. The selenation reaction is much faster than the geranylation of the corresponding 2-thiouridine-anticodon-stem-loop fragment
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: ybbB is required in vivo for the specific substitution of selenium for sulfur in 2-thiouridine residues in Escherichia coli tRNA. This modified tRNA nucleoside, 5-methylaminomethyl-2-selenouridine (mnm5se2U), is located at the wobble position of the anticodons of tRNALys, tRNAGlu, and tRNA1Gln
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: the enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: overall reaction. Reaction with tRNA anticodon-stem-loop fragments. The enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA. The selenation reaction is much faster than the geranylation of the corresponding 2-thiouridine-anticodon-stem-loop fragment
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Escherichia coli TL524
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Escherichia coli TL524
-
Substrates: ybbB is required in vivo for the specific substitution of selenium for sulfur in 2-thiouridine residues in Escherichia coli tRNA. This modified tRNA nucleoside, 5-methylaminomethyl-2-selenouridine (mnm5se2U), is located at the wobble position of the anticodons of tRNALys, tRNAGlu, and tRNA1Gln
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: the enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: the enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: ybbB is required in vivo for the specific substitution of selenium for sulfur in 2-thiouridine residues in Escherichia coli tRNA. This modified tRNA nucleoside, 5-methylaminomethyl-2-selenouridine (mnm5se2U), is located at the wobble position of the anticodons of tRNALys, tRNAGlu, and tRNA1Gln
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: the enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Escherichia coli TL524
-
Substrates: ybbB is required in vivo for the specific substitution of selenium for sulfur in 2-thiouridine residues in Escherichia coli tRNA. This modified tRNA nucleoside, 5-methylaminomethyl-2-selenouridine (mnm5se2U), is located at the wobble position of the anticodons of tRNALys, tRNAGlu, and tRNA1Gln
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O
5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate
Substrates: the enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0171
Selenophosphate
-
pH 7.2, 37Ā°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
evolution
-
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
evolution
-
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
evolution
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
evolution
-
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
evolution
-
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
evolution
-
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
evolution
-
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
evolution
-
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
evolution
-
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
evolution
-
the putative bipartite ortholog of the bacterial YbbB gene is identified in twelve additional archaeal genomes. Its function is confirmed as a tRNA 2-selenouridine synthase through biochemical and genetic experiments. A phylogenetic analysis of bacterial and archaeal versions of this enzyme provides insights into the early evolution of tRNA 2-selenouridine synthase. The active site loop containing the YbbB-characteristic CXRGGXRS motif near the C-terminus of the rhodanese domain and the Walker A motif (GX4GKT) at the N-terminus of the P-loop domain are highly conserved among the archaeal and bacterial YbbB sequences. The identified archaeal YbbB orthologs represent a bipartite version of bacterial tRNA 2-selenouridine synthase
malfunction
-
an Escherichia coli mutant deficient in ybbB is incapable of incorporating selenium into tRNA
malfunction
Escherichia coli TL524
-
an Escherichia coli mutant deficient in ybbB is incapable of incorporating selenium into tRNA
-
Show AA Sequence and Transmembrane Helices (3737 entries)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C96S
-
wild-type enzyme and mutant enzyme C96S produce similar amounts of 75Se-labeled tRNA
C96S
Escherichia coli TL524
-
wild-type enzyme and mutant enzyme C96S produce similar amounts of 75Se-labeled tRNA
-
G67E
mutation in the rhodanese domain increases the intrinsic low geranylation activity of the wild type MnmH
G67E/K155A
the mutant enzyme does not transfer in vitro a geranyl group from geranylpyrophosphate to tRNA
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sierant, M.; Leszczynska, G.; Sadowska, K.; Komar, P.; Radzikowska-Cieciura, E.; Sochacka, E.; Nawrot, B.
Escherichia coli tRNA 2-selenouridine synthase (SelU) converts S2U-RNA to Se2U-RNA via S-geranylated-intermediate
FEBS Lett.
592
2248-2258
2018
Escherichia coli (P33667), Escherichia coli, Escherichia coli K12 (P33667)
brenda
Jager, G.; Chen, P.; Bjork, G.R.
Transfer RNA bound to mnmh protein is enriched with geranylated tRNA-a possible intermediate in its selenation
PLoS One
11
e0153488
2016
Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZR88), Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Su, D.; Ojo, T.T.; Soell, D.; Hohn, M.J.
Selenomodification of tRNA in archaea requires a bipartite rhodanese enzyme
FEBS Lett.
586
717-721
2012
Methanocaldococcus jannaschii, Methanococcus aeolicus, Methanococcus maripaludis, Methanococcus maripaludis (Q6LYT8), Methanococcus vannielii, Methanococcus voltae, Methanocaldococcus fervens, Methanocaldococcus infernus, Methanocaldococcus vulcanius, Methanocaldococcus sp. FS406-22, Methanothermococcus okinawensis
brenda
Wolfe, M.D.; Ahmed, F.; Lacourciere, G.M.; Lauhon, C.T.; Stadtman, T.C.; Larson, T.J.
Functional diversity of the rhodanese homology domain the Escherichia coli ybbB gene encodes a selenophosphate-dependent tRNA 2-selenouridine synthase
J. Biol. Chem.
279
1801-1809
2004
Escherichia coli, Escherichia coli TL524
brenda
Veres, Z.; Stadtman, T.C.
A purified selenophosphate-dependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium
Proc. Natl. Acad. Sci. USA
91
8092-8096
1994
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
EXTERNAL LINKS (specific for EC-Number 2.9.1.3)
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Release 2023.1 (January 2023)
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