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Information on EC 2.8.1.13 - tRNA-uridine 2-sulfurtransferase and Organism(s) Escherichia coli and UniProt Accession P25745
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2.8.1.13 tRNA-uridine 2-sulfurtransferaseIUBMB Comments
The enzyme, found in bacteria, catalyses formation of the 2-thiouridine modification in the wobble position of tRNAGln, tRNALys and tRNAGlu.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
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a [protein]-S-sulfanyl-L-cysteine
+
uacil34 in tRNA
+
+
=
a [protein]-L-cysteine
+
2-thiouracil34 in tRNA
+
+
+
Synonyms
MnmA, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [protein]-S-sulfanyl-L-cysteine + uacil34 in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 2-thiouracil34 in tRNA + AMP + diphosphate + acceptor
on enzyme activation, an alpha-helix overhanging the active site is restructured into an idiosyncratic beta-hairpin-containing loop, which packs the flipped-out U34 deeply into the catalytic pocket and triggers the activation of the catalytic cysteine residues. The adenylated RNA intermediate is trapped. The active closed-conformation of the complex ensures accurate sulfur incorporation into the activated uridine carbon by forming a catalytic chamber to prevent solvent from accessing the catalytic site
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
[protein]-S-sulfanyl-L-cysteine:tRNA (uridine34-2-O)-sulfurtransferase
The enzyme, found in bacteria, catalyses formation of the 2-thiouridine modification in the wobble position of tRNAGln, tRNALys and tRNAGlu.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor
-
the enzyme functions on tRNALys(mnm5s2UUU), tRNAGlu(mnm5s2UUC), and tRNAGln((c)mnm5s2UUG)
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-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
-
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
MnmA catalyzes a sulfuration reaction to synthesize 2-thiouridine at the wobble positions of tRNAGlu, tRNAGln and tRNALys in Escherichia coli
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
the biogenesis of 2-thiouridine in Escherichia coli utilizes persulfide chemistry and proceeds through a complex sulfur-relay system by multiple sulfur mediators that select and facilitate specific sulfur flow to 2-thiouridine from various cellular sulfur pathways. TusE interacts with MnmA, a thiouridylase responsible for 2-thiouridine formation, and transfers the persulfide to it. MnmA activates the C2-position of the uracil base at the wobble position of the tRNA by forming an acyl-adenylated intermediate. Then, nucleophilic attack by the persulfide sulfur on the activated carbon generates a thiocarbonyl group by releasing the AMP
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
the wobble bases of bacterial tRNAs responsible for NNR codons are modified to 5-methylaminomethyl-2-thiouridine (mnm5s2U). 2-thio modification of mnm5s2U is required for accurate decoding and essential for normal cell growth. IscS and MnmA are the minimum essential factors for 2-thiolation of mnm5s2U in vitro. TusE directly interacts with MnmA-tRNA to form a ternary complex. TusE appears to interact with MnmA, but not with tRNA, because TusE-tRNA interactions are not observed
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
TusE interacts with MnmA, a thiouridylase responsible for 2-thiouridine formation, and transfers the persulfide to it. MnmA activates the C2-position of the uracil base at the wobble position of the tRNA by forming an acyl-adenylated intermediate. Then, nucleophilic attack by the persulfide sulfur on the activated carbon generates a thiocarbonyl group by releasing the AMP
-
-
?
additional information
?
-
thionucleosides are uniquely present in tRNA. In many organisms, tRNAs specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome binding ability to tRNA and improves reading frame maintenance
-
-
?
additional information
?
-
thionucleosides are uniquely present in tRNA. In many organisms, tRNAs specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. Purified IscS-persulfide is able to provide sulfur for in vitro s2U synthesis in the absence of cysteine. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome binding ability to tRNA and improves reading frame maintenance. Identification of 2-thiouridine as product of the in vitro s2U reaction.
-
-
?
additional information
?
-
-
in the IscSeMnmA pathway, protein MnmA, together with the cysteine desulfurase IscS and sulfur transfer mediators TusA-E, performs thiolation at position 2 of U34, which occurs only in tRNALys mnm5s2UUU, tRNAGlu mnm5s2UUC, tRNAGln cmnm5s2UUG
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor
-
the enzyme functions on tRNALys(mnm5s2UUU), tRNAGlu(mnm5s2UUC), and tRNAGln((c)mnm5s2UUG)
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
MnmA catalyzes a sulfuration reaction to synthesize 2-thiouridine at the wobble positions of tRNAGlu, tRNAGln and tRNALys in Escherichia coli
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
the biogenesis of 2-thiouridine in Escherichia coli utilizes persulfide chemistry and proceeds through a complex sulfur-relay system by multiple sulfur mediators that select and facilitate specific sulfur flow to 2-thiouridine from various cellular sulfur pathways. TusE interacts with MnmA, a thiouridylase responsible for 2-thiouridine formation, and transfers the persulfide to it. MnmA activates the C2-position of the uracil base at the wobble position of the tRNA by forming an acyl-adenylated intermediate. Then, nucleophilic attack by the persulfide sulfur on the activated carbon generates a thiocarbonyl group by releasing the AMP
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
the wobble bases of bacterial tRNAs responsible for NNR codons are modified to 5-methylaminomethyl-2-thiouridine (mnm5s2U). 2-thio modification of mnm5s2U is required for accurate decoding and essential for normal cell growth. IscS and MnmA are the minimum essential factors for 2-thiolation of mnm5s2U in vitro. TusE directly interacts with MnmA-tRNA to form a ternary complex. TusE appears to interact with MnmA, but not with tRNA, because TusE-tRNA interactions are not observed
-
-
?
additional information
?
-
thionucleosides are uniquely present in tRNA. In many organisms, tRNAs specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome binding ability to tRNA and improves reading frame maintenance
-
-
?
additional information
?
-
-
in the IscSeMnmA pathway, protein MnmA, together with the cysteine desulfurase IscS and sulfur transfer mediators TusA-E, performs thiolation at position 2 of U34, which occurs only in tRNALys mnm5s2UUU, tRNAGlu mnm5s2UUC, tRNAGln cmnm5s2UUG
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-
?
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the MnmA thiouridylaseĀtRNA(Glu) binary complex in three discrete forms, which provide snapshots of the sequential chemical reactions during RNA sulfuration
hanging-drop vapour-diffusion method, the binary complex of MnmA and tRNAGlu is crystallized in two different crystal forms: forms I and II. Cocrystallization of MnmAĀtRNAGlu with ATP yields form III crystals. The three crystal forms diffracted to 3.1 A, 3.4 A and 3.4 A resolution, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kambampati, R.; Lauhon, C.T.
MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli
Biochemistry
42
1109-1117
2003
Escherichia coli (P25745)
Numata, T.; Ikeuchi, Y.; Fukai, S.; Suzuki, T.; Nureki, O.
Snapshots of tRNA sulphuration via an adenylated intermediate
Nature
442
419-424
2006
Escherichia coli (P25745)
Numata, T.; Ikeuchi, Y.; Fukai, S.; Adachi, H.; Matsumura, H.; Takano, K.; Murakami, S.; Inoue, T.; Mori, Y.; Sasaki, T.; Suzuki, T.; Nureki, O.
Crystallization and preliminary X-ray analysis of the tRNA thiolation enzyme MnmA from Escherichia coli complexed with tRNA(Glu)
Acta Crystallogr. Sect. F
62
368-371
2006
Escherichia coli (P25745)
Ikeuchi, Y.; Shigi, N.; Kato, J.; Nishimura, A.; Suzuki, T.
Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions.
Mol. Cell
21
97-108
2006
Escherichia coli (P25745)
Noma, A.; Sakaguchi, Y.; Suzuki, T.
Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions
Nucleic Acids Res.
37
1335-1352
2009
Escherichia coli (P25745)
Naumann, P.-T.
Versuche zur Strukturaufklärung bakterieller Thiouridin Synthetasen
PH. D. Thesis Universität Göttingen
2005
0000
2005
Escherichia coli (P25745), Thermotoga maritima
-
Armengod, M.E.; Moukadiri, I.; Prado, S.; Ruiz-Partida, R.; Benitez-Paez, A.; Villarroya, M.; Lomas, R.; Garzon, M.J.; Martinez-Zamora, A.; Meseguer, S.; Navarro-Gonzalez, C.
Enzymology of tRNA modification in the bacterial MnmEG pathway
Biochimie
94
1510-1520
2012
Escherichia coli
Armengod, M.E.; Meseguer, S.; Villarroya, M.; Prado, S.; Moukadiri, I.; Ruiz-Partida, R.; Garzon, M.J.; Navarro-Gonzalez, C.; Martinez-Zamora, A.
Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes
RNA Biol.
11
1495-1507
2014
Escherichia coli
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