Any feedback?
No. of entries
Information on EC 2.1.1.167 - 27S pre-rRNA (guanosine2922-2'-O)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.167
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.167 27S pre-rRNA (guanosine2922-2'-O)-methyltransferase
IUBMB Comments
Spb1p is a site-specific 2′-O-ribose RNA methyltransferase that catalyses the formation of 2′-O-methylguanosine2922, a universally conserved position of the catalytic center of the ribosome that is essential for translation. 2′-O-Methylguanosine2922 is formed at a later stage of the processing, during the maturation of of the 27S pre-rRNA. In absence of snR52, Spb1p can also catalyse the formation of uridine2921 .
The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae
- 2.1.1.167
- rrnas
-
nucleolar
-
2'-o-ribose
-
pre-ribosomal
-
coimmunoprecipitation
-
cold-sensitive
- methyltransferases
Reaction Schemes
show+
=
+
+
guanosine2922 in 27S pre-rRNA
=
+
2'-O-methylguanosine2922 in 27S pre-rRNA
Synonyms
spb1p, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Spb1p
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanosine2922 in 27S pre-rRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine2922 in 27S pre-rRNA
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:27S pre-rRNA (guanosine2922-2'-O)-methyltransferase
Spb1p is a site-specific 2'-O-ribose RNA methyltransferase that catalyses the formation of 2'-O-methylguanosine2922, a universally conserved position of the catalytic center of the ribosome that is essential for translation. 2'-O-Methylguanosine2922 is formed at a later stage of the processing, during the maturation of of the 27S pre-rRNA. In absence of snR52, Spb1p can also catalyse the formation of uridine2921 [1].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + guanosine2922 in 27S pre-rRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine2922 in 27S pre-rRNA
-
Substrates: Spb1p is a site-specific 2'-O-ribose RNA MTase that catalyzes the formation of Gm2922, a universally conserved position of the catalytic center of the ribosome that is essential for translation. The enzyme is required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation. 2'-O-methylguanosine2922 appears at a late processing stage, during the maturation of the 27S pre-rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2918 in 25S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
S-adenosyl-L-methionine + uridine2918 in 25S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
Substrates: the enzyme is required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2918 in 25S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
-
Substrates: the enzyme is required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2918 in 25S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
Substrates: no methylation of uridine2791
Products: -
Products: -
?
additional information
?
-
Substrates: Spb1p is required for proper assembly of pre-ribosomal particles during the biogenesis of 60S ribosomal subunits
Products: -
Products: -
?
additional information
?
-
-
Substrates: Spb1p is required for proper assembly of pre-ribosomal particles during the biogenesis of 60S ribosomal subunits
Products: -
Products: -
?
additional information
?
-
Substrates: a point mutation in the Ado-Met binding site of Spb1p affects cell growth but does not abolish methylation of U2918. When this mutation is combined with disruption of snR52 cell growth is severely impaired and U2918 is no longer methylated. In vitro, Spb1p is able to methylate U2918 on 60S subunits. For this methylation two mechanisms coexist: a site-specific methyltransferase (Spb1p) and a snoRNA-dependent mechanism
Products: -
Products: -
?
additional information
?
-
-
Substrates: a point mutation in the Ado-Met binding site of Spb1p affects cell growth but does not abolish methylation of U2918. When this mutation is combined with disruption of snR52 cell growth is severely impaired and U2918 is no longer methylated. In vitro, Spb1p is able to methylate U2918 on 60S subunits. For this methylation two mechanisms coexist: a site-specific methyltransferase (Spb1p) and a snoRNA-dependent mechanism
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + guanosine2922 in 27S pre-rRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine2922 in 27S pre-rRNA
-
Substrates: Spb1p is a site-specific 2'-O-ribose RNA MTase that catalyzes the formation of Gm2922, a universally conserved position of the catalytic center of the ribosome that is essential for translation. The enzyme is required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation. 2'-O-methylguanosine2922 appears at a late processing stage, during the maturation of the 27S pre-rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2918 in 25S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
S-adenosyl-L-methionine + uridine2918 in 25S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
Substrates: the enzyme is required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2918 in 25S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
-
Substrates: the enzyme is required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation
Products: -
Products: -
?
additional information
?
-
Substrates: Spb1p is required for proper assembly of pre-ribosomal particles during the biogenesis of 60S ribosomal subunits
Products: -
Products: -
?
additional information
?
-
-
Substrates: Spb1p is required for proper assembly of pre-ribosomal particles during the biogenesis of 60S ribosomal subunits
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
Spb1p possesses a putative S-adenosyl-L-methionine-binding domain, which is common to the S-adenosyl-L-methionine-dependent methyltransferases
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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
malfunction
malfunction
a point mutation in the Ado-Met binding site of Spb1p affects cell growth but does not abolish methylation of U2918. When this mutation is combined with disruption of snR52 cell growth is severely impaired and U2918 is no longer methylated. In vitro, Spb1p is able to methylate U2918 on 60S subunits. For this methylation two mechanisms coexist: a site-specific methyltransferase (Spb1p) and a snoRNA-dependent mechanism
malfunction
in an spb1-2 strain grown at the restrictive temperature, processing of the 27S prerRNA into mature 25S rRNA and 5.8S is completely abolished and production of mature 18S is reduced, while the abnormal 23S species is accumulated
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SPB1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
841
0
96485
Swiss-Prot
-
NOG1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
647
0
74410
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D52A
-
when the mutant protein is the sole source of Spb1p in the cell (strain YBL4637), it leads to a severe growth defect with a generation time of about 300 min. No formation of 2'-O-methylguanosine2922
additional information
additional information
a point mutation in the Ado-Met binding site of Spb1p affects cell growth but does not abolish methylation of U2918. When this mutation is combined with disruption of snR52 cell growth is severely impaired and U2918 is no longer methylated. In vitro, Spb1p is able to methylate U2918 on 60S subunits. For this methylation two mechanisms coexist: a site-specific methyltransferase (Spb1p) and a snoRNA-dependent mechanism
additional information
-
a point mutation in the Ado-Met binding site of Spb1p affects cell growth but does not abolish methylation of U2918. When this mutation is combined with disruption of snR52 cell growth is severely impaired and U2918 is no longer methylated. In vitro, Spb1p is able to methylate U2918 on 60S subunits. For this methylation two mechanisms coexist: a site-specific methyltransferase (Spb1p) and a snoRNA-dependent mechanism
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pintard, L.; Kressler, D.; Lapeyre, B.
Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine in vitro
Mol. Cell. Biol.
20
1370-1381
2000
Saccharomyces cerevisiae (P25582), Saccharomyces cerevisiae
brenda
Bonnerot, C.; Pintard, L.; Lutfalla, G.
Functional redundancy of Spb1p and a snR52-dependent mechanism for the 2'-O-ribose methylation of a conserved rRNA position in yeast
Mol. Cell
12
1309-1315
2003
Saccharomyces cerevisiae (P25582), Saccharomyces cerevisiae
brenda
Lapeyre, B.; Purushothaman, S.K.
Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage
Mol. Cell
16
663-669
2004
Saccharomyces cerevisiae
brenda
Kressler, D.; Rojo, M.; Linder P.; Cruz, J.
Spb1p is a putative methyltransferase required for 60S ribosomal subunit biogenesis in Saccharomyces cerevisiae
Nucleic Acids Res.
27
4598-4608
1999
Saccharomyces cerevisiae (P25582), Saccharomyces cerevisiae
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.167)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
