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Information on EC 2.1.1.218 - tRNA (adenine9-N1)-methyltransferase and Organism(s) Homo sapiens and UniProt Accession Q7L0Y3

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.218 tRNA (adenine9-N1)-methyltransferase
IUBMB Comments
The enzyme from Sulfolobus acidocaldarius specifically methylates adenine9 in tRNA . The bifunctional enzyme from Thermococcus kodakaraensis also catalyses the methylation of guanine9 in tRNA (cf. EC 2.1.1.221, tRNA (guanine9-N1)-methyltransferase).
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This record set is specific for:
Homo sapiens
UNIPROT: Q7L0Y3
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
Synonyms
trmt10b, htrmt10b, adenosine-specific trm10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SPOUT MTase
-
tRNA m1A9 methyltransferase
-
tRNA m1R9 methyltransferase
-
additional information
see also EC 2.1.1.221
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (adenine9-N1)-methyltransferase
The enzyme from Sulfolobus acidocaldarius specifically methylates adenine9 in tRNA [1]. The bifunctional enzyme from Thermococcus kodakaraensis also catalyses the methylation of guanine9 in tRNA (cf. EC 2.1.1.221, tRNA (guanine9-N1)-methyltransferase).
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 + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + adenine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAArg
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNAAsp
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAAsp
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNATrp
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNATrp
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 + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
show the reaction diagram
-
the Watson-Crick base-pair-disrupting methyl group N1-methyladenine9 is sufficient for cloverleaf folding of human mitochondrial tRNALys
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAArg
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNAAsp
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAAsp
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNATrp
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNATrp
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
evolution
the enzyme belongs to the tRNA m1R9 methyltransferase (Trm10) family, which is conserved throughout eukarya and archaea. Distinct substrate specificities of the human tRNA methyltransferases TRMT10A and TRMT10B. hTRMT10A and hTRMT10B are not biochemically redundant. hTRMT10A is the de facto methyltransferase responsible for all m1G9 formation on cytosolic tRNA, and hTRMT10B has a much more limited and specific role in tRNA processing in humans
physiological function
hTRMT10B exhibits a restricted selectivity unusual for the Trm10 enzyme family
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TM10C_HUMAN
403
0
47347
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G231R
site-directed mutagenesis, the mutation abolishs methylation of tRNAAsp and tRNATrp, with some residual (though reduced) activity on tRNAArg
G231R/G232R
site-directed mutagenesis, the double mutant displays no methylation activity on any of the three substrates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Helm, M.; Gieg, R.; Florentz, C.
A Watson-Crick base-pair-disrupting methyl group (m1A9) is sufficient for cloverleaf folding of human mitochondrial tRNALys
Biochemistry
38
13338-13346
1999
Homo sapiens
Manually annotated by BRENDA team
Oerum, S.; Degut, C.; Barraud, P.; Tisne, C.
m1A Post-transcriptional modification in tRNAs
Biomolecules
7
20
2017
Homo sapiens (Q7L0Y3), Sulfolobus acidocaldarius (Q4J894), Sulfolobus acidocaldarius ATCC 33909 (Q4J894), Sulfolobus acidocaldarius DSM 639 (Q4J894), Sulfolobus acidocaldarius JCM 8929 (Q4J894), Sulfolobus acidocaldarius NBRC 15157 (Q4J894), Sulfolobus acidocaldarius NCIMB 11770 (Q4J894), Thermococcus kodakarensis (Q5JD38), Thermococcus kodakarensis ATCC BAA-918 (Q5JD38), Thermococcus kodakarensis JCM 12380 (Q5JD38)
Manually annotated by BRENDA team
Howell, N.; Jora, M.; Jepson, B.; Limbach, P.; Jackman, J.
Distinct substrate specificities of the human tRNA methyltransferases TRMT10A and TRMT10B
RNA
25
1366-1376
2019
Homo sapiens (Q6PF06), Homo sapiens
Manually annotated by BRENDA team