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Information on EC 2.8.1.4 - tRNA uracil 4-sulfurtransferase and Organism(s) Escherichia coli and UniProt Accession P25745

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.1 Sulfurtransferases
                2.8.1.4 tRNA uracil 4-sulfurtransferase
IUBMB Comments
The enzyme, found in bacteria and archaea, is activated by EC 2.8.1.7, cysteine desulfurase, which transfers a sulfur atom to an internal L-cysteine residue, forming a cysteine persulfide. The activated enzyme then transfers the sulfur to a uridine in a tRNA chain in a reaction that requires ATP. The enzyme from the bacterium Escherichia coli forms 4-thiouridine only at position 8 of tRNA. The enzyme also participates in the biosynthesis of the thiazole moiety of thiamine, but different domains are involved in the two processes.
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Escherichia coli
UNIPROT: P25745
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
thiouridylase, mmp1354, rna sulfurtransferase, transfer rna sulfurtransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ribonucleate sulfurtransferase
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-
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RNA sulfurtransferase
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transfer ribonucleate sulfurtransferase
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transfer RNA sulfurtransferase
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transferRNA thiolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + uracil in tRNA + 2 reduced ferredoxin [iron-sulfur] cluster = AMP + diphosphate + 4-thiouracil in tRNA + [ThiI sulfur-carrier protein]-L-cysteine + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfur atom transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine:uracil in tRNA sulfurtransferase
The enzyme, found in bacteria and archaea, is activated by EC 2.8.1.7, cysteine desulfurase, which transfers a sulfur atom to an internal L-cysteine residue, forming a cysteine persulfide. The activated enzyme then transfers the sulfur to a uridine in a tRNA chain in a reaction that requires ATP. The enzyme from the bacterium Escherichia coli forms 4-thiouridine only at position 8 of tRNA. The enzyme also participates in the biosynthesis of the thiazole moiety of thiamine, but different domains are involved in the two processes.
CAS REGISTRY NUMBER
COMMENTARY hide
9055-57-6
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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
L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
show the reaction diagram
L-cysteine + E. coli 'activated' tRNA
L-serine + tRNA containing a thionucleotide
show the reaction diagram
L-cysteine + poly A-2poly U
L-serine + S-tRNA
show the reaction diagram
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-
-
-
?
L-cysteine + poly A-poly U
L-serine + S-tRNA
show the reaction diagram
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-
-
-
?
L-cysteine + poly G,U
L-serine + S-tRNA
show the reaction diagram
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G:U = 2
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-
?
L-cysteine + Saccharomyces cerevisiae 'activated' tRNA
L-serine + tRNA containing a thionucleotide
show the reaction diagram
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same activity with baker's yeast tRNA as RNA acceptor
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r
L-cysteine + tRNA
?
show the reaction diagram
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?
additional information
?
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2-thiocytidine is the major thionucleotide formed in vitro, 4-thiouridine is the major product in vivo
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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
L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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beta-mercaptopyruvate is inactive either as a cofactor or as a sulfur donor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cd2+
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inhibits the synthesis of s4U
Co2+
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inhibits the synthesis of s4U
Fe2+
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inhibits the synthesis of s4U
Ni2+
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inhibits the synthesis of s4U
Zn2+
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inhibits the synthesis of s4U
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.26
L-cysteine
0.0027
tRNA
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pH 7.5, 37°C, sulfur deficient tRNA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with tRNAGlu
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, partly purified pooled protein fractions can be stored indefinitely for periods up to several months
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4°C, addition of toluene, can be stored indefinitely for periods up to several months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sulfurtransferase system with 2 enzymes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abrell, J.W.; Kaufman, E.E.; Lipsett, M.N.
The biosynthesis of 4-thiouridylate. Separation and purification of two enzymes in the transfer ribonucleic acid-sulfurtransferase system
J. Biol. Chem.
246
294-301
1971
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Harris, C.L.; Titchener, E.B.
Sulfur-deficient transfer ribonucleic acid. The natural substrate for ribonucleic acid sulfurtransferase from Escherichia coli
Biochemistry
10
4207-4212
1971
Escherichia coli, Escherichia coli HfrC
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team