Information on EC 2.8.4.4 - [ribosomal protein S12] (aspartate89-C3)-methylthiotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.8.4.4
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RECOMMENDED NAME
GeneOntology No.
[ribosomal protein S12] (aspartate89-C3)-methylthiotransferase
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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
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
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
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Escherichia coli W3110 / ATCC 27325
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3,3-bismethylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
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
Asp89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
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
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-
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-
?
L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor
3-methylthio-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
show the reaction diagram
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-
-
-
?
L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced acceptor
3-methylthio-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
show the reaction diagram
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-
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ir
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
-
-
-
?
L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor
3-methylthio-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
show the reaction diagram
-
-
-
-
?
L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced acceptor
3-methylthio-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
show the reaction diagram
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ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
[4Fe-4S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
[4Fe-4S]-center
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the enzyme binds two [4Fe-4S] clusters. The sulfur donor is believed to be one of the [4Fe-4S] clusters
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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assay at
PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49582
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x * 49582, calculated from nucleotide sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 49582, calculated from nucleotide sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.0 A crystal structure of the central radical S-adenosyl-L-methionine and the C-terminal tRNA methyltransferase 2 and MiaB domainsTRAM in apo-RimO. Although the core of the open TIM barrel of the radical S-adenosyl-L-methionine domain is conserved, RimO shows differences in domain organization compared with other radical S-adenosyl-L-methionine enzymes. The unusually acidicTRAM domain, likely to bind the basic S12 protein, is located at the distal edge of the radical AdoMet domain. The basic S12 protein substrate is likely to bind RimO through interactions with both the TRAM domain and the concave surface of the incomplete TIM barrel
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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