EC Tree |
2. Transferases |
2.4 Glycosyltransferases |
2.4.99 Transferring other glycosyl groups |
ID: | 2.4.99.17 |
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Description: | S-adenosylmethionine:tRNA ribosyltransferase-isomerase. |
Alternative Name: |
Queuosine biosynthesis protein QueA. |
Cath: | 2.40.10.240; 3.40.1780.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.4.99.17 |
BRENDA Enzyme Link: | BRENDA 2.4.99.17 |
KEGG Enzyme Link: | KEGG2.4.99.17 |
BioCyc Enzyme Link: | BioCyc 2.4.99.17 |
ExPASy Enzyme Link: | ExPASy2.4.99.17 |
EC2PDB Enzyme Link: | EC2PDB 2.4.99.17 |
ExplorEnz Enzyme Link: | ExplorEnz 2.4.99.17 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.4.99.17 |
IntEnz Enzyme Link: | IntEnz 2.4.99.17 |
MEDLINE Enzyme Link: | MEDLINE 2.4.99.17 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:32155 | 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-methionine |
RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH2;+0:6]-[*:7]-[O;H0;+0:8]-[CH;+0:9](-[*:10])-[n;H0;+0:11](:[*:12]):[*:13]>>[*:1]-[NH;+0:2]-[CH;+0:9](-[*:10])-[CH;+0:6]1-[*:7]-[O;H0;+0:8]-1.[*:3]-[S;H0;+0:4]-[*:5].[*:12]:[nH;+0:11]:[*:13] |
Reaction | ![]() |
Core-to-Core | |
Core-to-Core | |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine. | Slany RK, Bösl M, Crain PF, Kersten H | 1993 Aug 3 | 8347586 |
Transfer and isomerization of the ribose moiety of AdoMet during the biosynthesis of queuosine tRNAs, a new unique reaction catalyzed by the QueA protein from Escherichia coli. | Slany RK, Bösl M, Kersten H | 1994 | 7849103 |
Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA). | Van Lanen SG, Iwata-Reuyl D | 2003 May 13 | 12731872 |
Mechanistic studies of the tRNA-modifying enzyme QueA: a chemical imperative for the use of AdoMet as a "ribosyl" donor. | Kinzie SD, Thern B, Iwata-Reuyl D | 2000 May 4 | 10810734 |