Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.167
Description:27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.167
BRENDA Enzyme Link: BRENDA 2.1.1.167
KEGG Enzyme Link: KEGG2.1.1.167
BioCyc Enzyme Link: BioCyc 2.1.1.167
ExPASy Enzyme Link: ExPASy2.1.1.167
EC2PDB Enzyme Link: EC2PDB 2.1.1.167
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.167
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.167
IntEnz Enzyme Link: IntEnz 2.1.1.167
MEDLINE Enzyme Link: MEDLINE 2.1.1.167
MSA:

2.1.1.167;

Phylogenetic Tree:

2.1.1.167;

Uniprot:
M-CSA:
RHEA:42724 guanosine(2922) in 27S pre-rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2922) in 27S pre-rRNA + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage.Lapeyre B, Purushothaman SK2004 Nov 1915546625
Functional redundancy of Spb1p and a snR52-dependent mechanism for the 2'-O-ribose methylation of a conserved rRNA position in yeast.Bonnerot C, Pintard L, Lutfalla G2003 Nov14636587