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Information on EC 2.1.1.257 - tRNA (pseudouridine54-N1)-methyltransferase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57977

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EC Tree
IUBMB Comments
While this archaeal enzyme is specific for the 54 position and does not methylate pseudouridine at position 55, the presence of pseudouridine at position 55 is necessary for the efficient methylation of pseudouridine at position 54 [2,3].
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This record set is specific for:
Methanocaldococcus jannaschii
UNIPROT: Q57977
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
cog1901, hvo_1989, pseudouridine n1-specific methyltransferase, duf358, duf358/mj1640, mja_1640, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pseudouridine-N1-specific methyltransferase
-
ribosome assembly factor Nep1
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m1-pseudouridine methyltransferase
-
m1PSI methyltransferase
-
-
-
-
pseudouridine N1-specific methyltransferase
-
SAM-dependent N1-pseudouridine methyltransferase
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TrmY
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (pseudouridine54-N1)-methyltransferase
While this archaeal enzyme is specific for the 54 position and does not methylate pseudouridine at position 55, the presence of pseudouridine at position 55 is necessary for the efficient methylation of pseudouridine at position 54 [2,3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + pseudouridine in 5'-GAUPsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-GAUmethylPsiCAACGCC-3'
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + pseudouridine in 5'-PsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-methylPsiCAACGCC-3'
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + pseudouridine in 5'-UPsiCAACGC--3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-UmethylPsiCAACGC--3'
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + pseudouridine in 5'-UPsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-UmethylPsiCAACGCC-3'
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
show the reaction diagram
additional information
?
-
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
S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
Nep1 structure reveals a dimer with a fold similar to the SPOUT-class of RNA-methyltransferases
physiological function
Nep1 acts as a methyltransferase in ribosome biogenesis
evolution
metabolism
Pus10-mediated PSI54 (and PSI55) formation does not require the presence of TrmY activity, overview
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
Nep1 structure reveals a dimer with a fold similar to the SPOUT-class of RNA-methyltransferases
dimer
Mj1640 forms a dimer, which is mediated by two parallel pairs of alpha-helices oriented almost perpendicular to each other
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and selenmethionine-labeled DUF358/Mj1640 in complex with S-adenosyl-L-methionine, at 20°C, mixing of 0.001 ml of protein solution with 0.001 l of reservoir containing 20% PEG 3350, 25 mM NH4F, 20 mM MgCl2, 100 mM Tris, pH 7.5, X-ray diffraction structure determination and analysis at 1.4 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and selenmethionine-labeled Mj1640 from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Mj1640, expression of wild-type and selenmethionine-labeled enzyme as N-terminally His-tagged protein in Escherichia coli strain Bl21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, H.; Yuan, Y.
Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase
J. Mol. Cell Biol.
2
366-374
2010
Methanocaldococcus jannaschii (Q59034), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Wurm, J.; Meyer, B.; Bahr, U.; Held, M.; Frolow, O.; Koetter, P.; Engels, J.; Heckel, A.; Karas, M.; Entian, K.; Woehnert, J.
The ribosome assembly factor Nep1 responsible for Bowen-Conradi syndrome is a pseudouridine-N1-specific methyltransferase
Nucleic Acids Res.
38
2387-2398
2010
Homo sapiens (Q92979), Homo sapiens, Methanocaldococcus jannaschii (Q57977), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57977)
Manually annotated by BRENDA team
Wurm, J.; Griese, M.; Bahr, U.; Held, M.; Heckel, A.; Karas, M.; Soppa, J.; Woehnert, J.
Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs
RNA
18
412-420
2012
Haloferax volcanii (D4GTL8), Haloferax volcanii, Methanocaldococcus jannaschii (Q59034), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Chatterjee, K.; Blaby, I.K.; Thiaville, P.C.; Majumder, M.; Grosjean, H.; Yuan, Y.A.; Gupta, R.; de Crecy-Lagard, V.
The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA
RNA
18
421-433
2012
Halobacterium sp. (Q9HNR6), Halobacterium sp., Halobacterium sp. NRC-1 (Q9HNR6), Haloferax volcanii (D4GTL8), Haloferax volcanii, Methanocaldococcus jannaschii (Q59034), Methanocaldococcus jannaschii
Manually annotated by BRENDA team