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Information on EC 2.1.1.33 - tRNA (guanine46-N7)-methyltransferase and Organism(s) Bacillus subtilis and UniProt Accession O34522

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.33 tRNA (guanine46-N7)-methyltransferase
IUBMB Comments
The enzyme specifically methylates guanine46 at N7 in tRNA.
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This record set is specific for:
Bacillus subtilis
UNIPROT: O34522
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
mettl1, methyltransferase like 1, m7g-methyltransferase, trna (m7g46) methyltransferase, m7g46 methyltransferase trm8p/trm82p, transfer rna (m7g46) methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tRNA (m7G46) methyltransferase
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7-methylguanine transfer ribonucleate methylase
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m7G-methyltransferase
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methyltransferase, transfer ribonucleate guanine 7-
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N7-methylguanine methylase
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transfer ribonucleate guanine 7-methyltransferase
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tRNA guanine 7-methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine-N7-)-methyltransferase
The enzyme specifically methylates guanine46 at N7 in tRNA.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-00-4
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
contains three potassium ions per asymmetric unit, one in the interface between monomers and one in a region involved in AdoMet binding in the homologous catechol O-MTase, bound to the main chain carbonyls of residues Asn115 and Gly46
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystallographic studies, gel filtration, dimeric both in crystal and in solution
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by hanging drop method, at a resolution of 2.1 A, Rossmann-fold methyltransferase structure with the N-terminal helix folded on the opposite site of the catalytic domain
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zegers, I.; Gigot, D.; van Vliet, F.; Tricot, C.; Aymerich, S.; Bujnicki, J.M.; Kosinski, J.; Droogmans, L.
Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase
Nucleic Acids Res.
34
1925-1934
2006
Bacillus subtilis (O34522), Bacillus subtilis
Manually annotated by BRENDA team