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Information on EC 2.8.4.4 - [ribosomal protein S12] (aspartate89-C3)-methylthiotransferase and Organism(s) Escherichia coli and UniProt Accession P0AEI4

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EC Tree
IUBMB Comments
This bacterial enzyme binds two [4Fe-4S] clusters [2,3]. A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters . In the first reaction the enzyme transfers a methyl group from AdoMet to the external sulfur ion of the sulfur bridge. In the second reaction the enzyme catalyses the reductive fragmentation of a second molecule of AdoMet, yielding a 5'-deoxyadenosine radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylsulfanyl group to aspartate89 [5,6]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes.
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This record set is specific for:
Escherichia coli
UNIPROT: P0AEI4
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Word Map
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  • 2.8.4.4
  • transposition
  • transposable
  • piggybac
  • protein-dna
  • cut-and-paste
  • integrases
  • transpososome
  • metnase
  • subterminal
  • nonautonomous
  • beauty
  • transposase-dna
  • helix-turn-helix
  • transposase-mediated
  • cointegrate
  • tpase
  • setmar
  • transgenesis
  • p-element
  • himar1
  • hermes
  • mariner-like
  • hobo
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
hide
L-aspartate89-[ribosomal protein S12]
+
sulfur-(sulfur carrier)
+
2
S-adenosyl-L-methionine
+
reduced acceptor
=
3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12]
+
S-adenosyl-L-homocysteine
+
(sulfur carrier)
+
L-methionine
+
5'-deoxyadenosine
+
oxidized acceptor
L-aspartate89-[ribosomal protein S12]
+
sulfur-(sulfur carrier)
+
2
+
=
3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12]
+
+
(sulfur carrier)
+
+
+
oxidized acceptor
S-adenosyl-L-methionine
+
L-aspartate89-[ribosomal protein S12]
+
sulfur-(sulfur carrier)
=
S-adenosyl-L-homocysteine
+
L-aspartate89-[ribosomal protein S12]-methanethiol
+
(sulfur carrier)
+
L-aspartate89-[ribosomal protein S12]
+
sulfur-(sulfur carrier)
=
+
L-aspartate89-[ribosomal protein S12]-methanethiol
+
(sulfur carrier)
L-aspartate89-[ribosomal protein S12]-methanethiol
+
S-adenosyl-L-methionine
+
reduced acceptor
=
3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12]
+
L-methionine
+
5'-deoxyadenosine
+
oxidized acceptor
L-aspartate89-[ribosomal protein S12]-methanethiol
+
+
=
3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12]
+
+
+
oxidized acceptor
Synonyms
ribosomal protein S12 methylthiotransferase, ribosome maturation factor RimO, RimO, S12 methylthiotransferase, yliG, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
show the reaction diagram
(overall reaction)
-
S-adenosyl-L-methionine + L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) = S-adenosyl-L-homocysteine + L-aspartate89-[ribosomal protein S12]-methanethiol + (sulfur carrier)
show the reaction diagram
(1a)
-
L-aspartate89-[ribosomal protein S12]-methanethiol + S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein S12] + L-methionine + 5'-deoxyadenosine + oxidized acceptor
show the reaction diagram
(1b)
-
SYSTEMATIC NAME
IUBMB Comments
[ribosomal protein S12]-Asp89:sulfur-(sulfur carrier),S-adenosyl-L-methionine C3-methylthiotransferase
This bacterial enzyme binds two [4Fe-4S] clusters [2,3]. A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters [6]. In the first reaction the enzyme transfers a methyl group from AdoMet to the external sulfur ion of the sulfur bridge. In the second reaction the enzyme catalyses the reductive fragmentation of a second molecule of AdoMet, yielding a 5'-deoxyadenosine radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylsulfanyl group to aspartate89 [5,6]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Asp88-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate88-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
substrate Escherichia coli S12 is modified at residue Asp88
-
-
?
Asp89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
-
-
-
-
?
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
Asp89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
the enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
[4Fe-4S]-center
-
the enzyme binds two [4Fe-4S] clusters. The sulfur donor is believed to be one of the [4Fe-4S] clusters
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49582
-
x * 49582, calculated from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 49582, calculated from nucleotide sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, K.H.; Saleh, L.; Anton, B.P.; Madinger, C.L.; Benner, J.S.; Iwig, D.F.; Roberts, R.J.; Krebs, C.; Booker, S.J.
Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily
Biochemistry
48
10162-10174
2009
Escherichia coli
Manually annotated by BRENDA team
Strader, M.; Costantino, N.; Elkins, C.; Chen, C.; Patel, I.; Makusky, A.; Choy, J.; Court, D.; Markey, S.; Kowalak, J.
A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein
Mol. Cell. Proteomics
10
M110.005199
2011
Escherichia coli (P0AEI4), Escherichia coli W3110 / ATCC 27325 (P0AEI4)
Manually annotated by BRENDA team
Anton, B.P.; Saleh, L.; Benner, J.S.; Raleigh, E.A.; Kasif, S.; Roberts, R.J.
RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli
Proc. Natl. Acad. Sci. USA
105
1826-1831
2008
Escherichia coli (P0AEI4)
Manually annotated by BRENDA team