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Information on EC 2.1.1.282 - tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase
for references in articles please use BRENDA:EC2.1.1.282
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.282 tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase
IUBMB Comments
The enzyme is involved in the biosynthesis of hypermodified tricyclic bases found at position 37 of certain tRNAs. These modifications are important for translational reading-frame maintenance. The enzyme is found in all eukaryotes and in some archaea, but not in bacteria. The eukaryotic enzyme is involved in the biosynthesis of wybutosine.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
showSynonyms
ygl050w, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aTrm5a methyltransferase
aTrm5a-type enzyme
SSO2439
Taw21
TAW22
Trm5a
tRNAPhe:imG2 methyltransferase
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe = S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
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PATHWAY SOURCE
PATHWAYS
MetaCyc
7-(3-amino-3-carboxypropyl)-wyosine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNAPhe 7-[(3S)-(3-amino-3-carboxypropyl)-4-demethylwyosine-N4]-methyltransferase
The enzyme is involved in the biosynthesis of hypermodified tricyclic bases found at position 37 of certain tRNAs. These modifications are important for translational reading-frame maintenance. The enzyme is found in all eukaryotes and in some archaea, but not in bacteria. The eukaryotic enzyme is involved in the biosynthesis of wybutosine.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)-4-demethyl]wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)-4-methyl]wyosine37 in tRNAPhe
Substrates: the enzyme is involved in the biosynthesis of the tricyclic base wybutosine
Products: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: i.e. im-G14, activity of EC 2.1.1.282
Products: -
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?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: i.e. im-G14, activity of EC 2.1.1.282
Products: -
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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: i.e. im-G14, activity of EC 2.1.1.282
Products: -
Products: -
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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: i.e. im-G14, activity of EC 2.1.1.282
Products: -
Products: -
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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: i.e. im-G14, activity of EC 2.1.1.282
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: i.e. im-G14, activity of EC 2.1.1.282
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: i.e. im-G14, activity of EC 2.1.1.282
Products: -
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S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
Substrates: -
Products: -
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S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
Substrates: i.e. yW-86, activity of EC 2.1.1.228
Products: -
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S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
Substrates: -
Products: -
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S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
Substrates: i.e. yW-86, activity of EC 2.1.1.228
Products: -
Products: -
?
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: imG-14
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
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additional information
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Substrates: Nanoarchaeum equitans NEQ228 protein displays a dual tRNAPhe:m1G/imG2 methyltransferase activity. Two different types of substrates are used: (1) bulk tRNA, isolated from Salmonella enterica trmDELTA27 mutant containing the unmodified G37 nucleotide leading to the formation of pm1G, and (2) tRNA, which is isolated from the Saccharomes cerevisiae DELTAtyw2 mutant that contains the imG-14 wyosine derivative leading to formation of pimG2pA dinucleotide and to a lesser extent to pm1G, likely resulting from the small amounts of G37-containing tRNAPhe present in the bulk tRNA isolates from the Scetyw2 mutant
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additional information
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Substrates: bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
Products: -
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additional information
?
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Substrates: bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
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additional information
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Substrates: Pyrococcus abyssi PAB2272 protein displays a dual tRNAPhe:m1G/imG2 methyltransferase activity. Two different types of substrates are used: (1) bulk tRNA, isolated from Salmonella enterica trmDELTA27 mutant containing the unmodified G37 nucleotide leading to the formation of pm1G, and (2) tRNA, which is isolated from the Saccharomes cerevisiae DELTAtyw2 mutant that contains the imG-14 wyosine derivative leading to formation of pimG2pA dinucleotide and to a lesser extent to pm1G, likely resulting from the small amounts of G37-containing tRNAPhe present in the bulk tRNA isolates from the Scetyw2 mutant
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additional information
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Substrates: structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA., the enzyme recognizes the overall shape of tRNA. PaTrm5a adopts distinct open conformations before and after the binding of tRNA. Enzyme-substrate interactions in the catalytic domain. The anticodon interactions mostly concentrate on the A36-G37-A38 triplet. Proposed reaction mechanism of Trm5a with modified yeast tRNAPhe, overview
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additional information
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Substrates: substrate-binding modes of PaTrm5a, and recognition of substrate analogues, overview
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additional information
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Substrates: Sulfolobus solfataricus SSO2439 protein exhibits a tRNAPhe:imG2, but not tRNAPhe:m1G (EC 2.1.1.228), methyltransferase activity. The enzyme SSO2439 shows incorporation of the [methyl-14C] group into bulk yeast tRNA isolated from Saccharomyces cerevisiae DELTAtyw2 (containing imG-14 in tRNAPhe), but not into that from the Salmonella enterica trmDELTA27 (containing G37) mutant
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additional information
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Substrates: Sulfolobus solfataricus SSO2439 protein exhibits a tRNAPhe:imG2, but not tRNAPhe:m1G (EC 2.1.1.228), methyltransferase activity. The enzyme SSO2439 shows incorporation of the [methyl-14C] group into bulk yeast tRNA isolated from Saccharomyces cerevisiae DELTAtyw2 (containing imG-14 in tRNAPhe), but not into that from the Salmonella enterica trmDELTA27 (containing G37) mutant
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additional information
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Substrates: Sulfolobus solfataricus SSO2439 protein exhibits a tRNAPhe:imG2, but not tRNAPhe:m1G (EC 2.1.1.228), methyltransferase activity. The enzyme SSO2439 shows incorporation of the [methyl-14C] group into bulk yeast tRNA isolated from Saccharomyces cerevisiae DELTAtyw2 (containing imG-14 in tRNAPhe), but not into that from the Salmonella enterica trmDELTA27 (containing G37) mutant
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additional information
?
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Substrates: Sulfolobus solfataricus SSO2439 protein exhibits a tRNAPhe:imG2, but not tRNAPhe:m1G (EC 2.1.1.228), methyltransferase activity. The enzyme SSO2439 shows incorporation of the [methyl-14C] group into bulk yeast tRNA isolated from Saccharomyces cerevisiae DELTAtyw2 (containing imG-14 in tRNAPhe), but not into that from the Salmonella enterica trmDELTA27 (containing G37) mutant
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additional information
?
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Substrates: Sulfolobus solfataricus SSO2439 protein exhibits a tRNAPhe:imG2, but not tRNAPhe:m1G (EC 2.1.1.228), methyltransferase activity. The enzyme SSO2439 shows incorporation of the [methyl-14C] group into bulk yeast tRNA isolated from Saccharomyces cerevisiae DELTAtyw2 (containing imG-14 in tRNAPhe), but not into that from the Salmonella enterica trmDELTA27 (containing G37) mutant
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)-4-demethyl]wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)-4-methyl]wyosine37 in tRNAPhe
Substrates: the enzyme is involved in the biosynthesis of the tricyclic base wybutosine
Products: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
Substrates: -
Products: -
Products: -
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additional information
?
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Substrates: bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
Products: -
Products: -
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additional information
?
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Substrates: bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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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
metabolism
physiological function
additional information
evolution
archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a ), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview
evolution
archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a ), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview. Crenarcheota Saccharolobus solfataricus as well as in other Sulfalobales and Desulfurococcales, two different tRNAPhe methyltransferases are involved in the biosynthesis of mimG, catalyzing the formation of m1G (Trm5c, EC 2.1.1.228) and imG2 (Trm5a, EC 2.1.1.282) at position 37 in tRNAPhe, respectively
evolution
archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview
evolution
during the evolutionary process, some euryarchaeota like Thermococcus and Pyrococcus preserved both the trm5 genes from the crenarchaeal origin as well as the native copy, but others apparently lost the latter. Phylogenetic distribution analyses of trm5 homologues in archaeal genomes allow the identification of three archaeal Trm5 (aTrm5) subfamilies: Trm5a, Trm5b, and Trm5c. Trm5b refers to the native form, while Trm5a refers to the crenarchaeal origin, and Trm5c to other members with divergent Trm5 sequences11. The three Trm5s differ substantially in primary sequences
evolution
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archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a ), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview. Crenarcheota Saccharolobus solfataricus as well as in other Sulfalobales and Desulfurococcales, two different tRNAPhe methyltransferases are involved in the biosynthesis of mimG, catalyzing the formation of m1G (Trm5c, EC 2.1.1.228) and imG2 (Trm5a, EC 2.1.1.282) at position 37 in tRNAPhe, respectively
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evolution
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archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a ), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview. Crenarcheota Saccharolobus solfataricus as well as in other Sulfalobales and Desulfurococcales, two different tRNAPhe methyltransferases are involved in the biosynthesis of mimG, catalyzing the formation of m1G (Trm5c, EC 2.1.1.228) and imG2 (Trm5a, EC 2.1.1.282) at position 37 in tRNAPhe, respectively
-
evolution
-
archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a ), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview. Crenarcheota Saccharolobus solfataricus as well as in other Sulfalobales and Desulfurococcales, two different tRNAPhe methyltransferases are involved in the biosynthesis of mimG, catalyzing the formation of m1G (Trm5c, EC 2.1.1.228) and imG2 (Trm5a, EC 2.1.1.282) at position 37 in tRNAPhe, respectively
-
evolution
-
archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a ), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview. Crenarcheota Saccharolobus solfataricus as well as in other Sulfalobales and Desulfurococcales, two different tRNAPhe methyltransferases are involved in the biosynthesis of mimG, catalyzing the formation of m1G (Trm5c, EC 2.1.1.228) and imG2 (Trm5a, EC 2.1.1.282) at position 37 in tRNAPhe, respectively
-
malfunction
in DELTATYW3 strain, tRNAPhe has two wybutosine intermediates, 7-(3-amino-3-carboxypropyl)-4-demethylwyosine37 (yW-86) and 4-demethylwyosine37 (yW-14). Recombinant TYW3 clearly methylated 7-(3-amino-3-carboxypropyl)-4-demethylwyosine37 in tRNA to yield 7-(3-amino-3-carboxypropyl)-4-methylwyosine37 in tRNA in S-adenosyl-L-methionine-dependent manner. 4-Demethylwyosine37 is not methylated by TYW3
malfunction
deletion of the D1 domain greatly reduces the affinity and activity of PaTrm5a toward its RNA substrate
malfunction
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
malfunction
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
malfunction
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
malfunction
-
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
-
malfunction
-
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
-
malfunction
-
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
-
malfunction
-
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
-
metabolism
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
metabolism
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
metabolism
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
metabolism
the enzyme is part of the biosynthetic pathway of mimG in Pyrococcus abyssi, overview. In archaea, G37 hypermodification in tRNAPhe leads to wyosine derivatives. They are important in reading-frame maintenance during protein synthesis, while the absence of such modifications results in elevated error rates in +1 frame-shifting. Among the modification products, 7-methylwyosine (mimG) is perhaps the earliest and minimalist version of the wyosine derivatives unique to some archaea, and 4-demethylwyosine (imG-14), isowyosine (imG2) have also been identified as intermediates along the pathway. The first biosynthetic step of mimG is the formation of m1G37, catalysed by the S-adenosine-L-methionine (SAM)-dependent tRNA methyltransferase named Trm5, which belongs to class-I methyltransferases. The second step is the complex radical-mediated formation of imG-14, catalyzed by the radical SAM enzyme Taw1. The Trm5 enzyme from the archaeon Pyrococcus abyssi (PaTrm5a) also catalyzes the methylation of C7 on imG-14 to produce imG2 (EC 2.1.1.282), which is further methylated on the N4 position of the imidazo-purine ring by Taw3 to form mimG
metabolism
-
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
-
metabolism
-
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
-
metabolism
-
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
-
metabolism
-
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
-
physiological function
the enzyme is involved in the biosynthesis of the tricyclic base wybutosine
physiological function
the methyltransferase Trm5a from Pyrococcus abyssi (PaTrm5a) plays a key role in this hypermodification process in generating m1G37 (EC 2.1.1.228) and imG2 (EC 2.1.1.282), two products of the wyosine biosynthetic pathway, through two methyl transfers to distinct substrates
physiological function
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
physiological function
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
physiological function
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
physiological function
tRNA methyltransferase Trm5 catalyses the transfer of a methyl group from S-adenosyl-L-methionine to G37 in eukaryotes and archaea. The N1-methylated guanosine is the product of the initial step of the wyosine hypermodification, which is essential for the maintenance of the reading frame during translation. As a unique member of this enzyme family, Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4-demethylwyosine at position 37 to produce isowyosine
physiological function
-
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
-
physiological function
-
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
-
physiological function
-
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
-
physiological function
-
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
-
physiological function
-
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
-
additional information
structure comparison of the Pyrococcus abyssii Trm5a enzyme structure (PDB ID 5WT1) with the structure of its orthologue Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii, overview
Show AA Sequence and Transmembrane Helices (2928 entries)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme structure analysis, he 38.5-kDa protein is composed of three domains: D1 (M1-P60), D2 (N70-S162) and D3 (K163-S333) D1 and D2 are connected through an interdomain linker (M61-K69), overview
additional information
substrate interactions with the catalytic region in the PaTrm5a-tRNAPhe-(imG-14)-SAH ternary complex, overview. In the model, imG-14 is flipped into a hydrophobic pocket formed by Phe165, Phe284, Tyr318, Met170, Tyr197, and the 260PTPK263 fragment
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant apo-PaTrm5a and PaTrm5a in complex with tRNAPhe, and PaTrm5a-tRNAPhe (imG-14)-SAH ternary complex, X-ray diffraction structure determination and analysis
purified recombinant PaTrm5a in apo form and in complex with various SAM analogues, mixing PaTrm5a with 1.5 mM SAH or SAM at a protein: ligand molar ratio of 1:3, sitting drop vapor diffusion method, mixing 20 mg/ml protein solution in a 1:1 ratio with well solution containing w/v PEG 3350, 100 mM HEPES, pH 7.5, 100 mM Ca(OAc)2 and 100 mM KCl., method optimmization, 25°C, X-ray diffraction structure determination and analysis at 1.76-2.20 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D243A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
E173A
site-directed mutagenesis, the mutant shows 9 and 26% of wild-type activity for imG and imG2 formation, respectively
E213A
H128A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
P260N
site-directed mutagenesis, the mutant shows no and 114% of wild-type activity for imG and imG2 formation, respectively
P262A
site-directed mutagenesis, the mutant shows 5 and 8% of wild-type activity for imG and imG2 formation, respectively
R133A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R134A
site-directed mutagenesis, the mutant shows 2 and 4% of wild-type activity for imG and imG2 formation, respectively
R135A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R174A
Y318A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
E213A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R174A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R174A
site-directed mutagenesis, the mutant shows 8 and 69% of wild-type activity for imG and imG2 formation, respectively
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme by affinity chromatography and desalting gel filtration
recombinant expression of His-tagged wild-type and mutant enzymes to near homogeneity by 20 min heat treatment at 70°C and 65°C, respectively, followed by affinity chromatography and desalting gel filtration
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and heparin affinity chromatography, and dialysis
recombinant expression of His-tagged enzyme by affinity chromatography and desalting gel filtration
recombinant expression of His-tagged enzyme by affinity chromatography and desalting gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene trm5a, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
hexahistidine-tagged enzyme is expressed in Saccharomyces cerevisiae
recombinant expression of His-tagged enzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noma, A.; Kirino, Y.; Ikeuchi, Y.; Suzuki, T.
Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA
EMBO J.
25
2142-2154
2006
Saccharomyces cerevisiae (P53177), Saccharomyces cerevisiae
brenda
Urbonavicius, J.; Rutkiene, R.; Lopato, A.; Tauraite, D.; Stankeviciute, J.; Aucynaite, A.; Kaliniene, L.; van Tilbeurgh, H.; Meskys, R.
Evolution of tRNAPhe imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea
RNA
22
1871-1883
2016
Nanoarchaeum equitans (Q74NE4), Pyrococcus abyssi (Q9V2G1), Pyrococcus abyssi Orsay (Q9V2G1), Saccharolobus solfataricus (Q97W08), Saccharolobus solfataricus ATCC 35092 (Q97W08), Saccharolobus solfataricus DSM 1617 (Q97W08), Saccharolobus solfataricus JCM 11322 (Q97W08), Saccharolobus solfataricus P2 (Q97W08)
brenda
Wang, C.; Jia, Q.; Zeng, J.; Chen, R.; Xie, W.
Structural insight into the methyltransfer mechanism of the bifunctional Trm5
Sci. Adv.
3
e1700195
2017
Pyrococcus abyssi (Q9V2G1)
brenda
Wang, C.; Jia, Q.; Chen, R.; Wei, Y.; Li, J.; Ma, J.; Xie, W.
Crystal structures of the bifunctional tRNA methyltransferase Trm5a
Sci. Rep.
6
33553
2016
Pyrococcus abyssi (Q9V2G1)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.282)
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Release 2023.1 (January 2023)
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