| Accession | TIGR00113 |
| Name | queA |
| Function | S-adenosylmethionine:tRNA ribosyltransferase-isomerase |
| Gene Symbol | queA |
| Trusted Cutoff | 267.45 |
| Domain Trusted Cutoff | 267.45 |
| Noise Cutoff | 158.00 |
| Domain Noise Cutoff | 158.00 |
| Isology Type | equivalog |
| EC Number | 2.4.99.17 |
| HMM Length | 345 |
| Mainrole Category | Protein synthesis |
| Subrole Category | tRNA and rRNA base modification |
| Gene Ontology Term | GO:0005737: cytoplasm cellular_component |
| | GO:0006400: tRNA modification biological_process |
| | GO:0008616: queuosine biosynthetic process biological_process |
| | GO:0051075: S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity molecular_function |
| Author | Anolik RT, Richardson DL |
| Entry Date | Apr 20 1999 2:09PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This model describes the enzyme for S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA). QueA synthesizes Queuosine which is usually in the first position of the anticodon of tRNAs specific for asparagine, aspartate, histidine, and tyrosine. |
| References | DR ECOCYC; EG10812;
DR InterPro; IPR003699; Queuosine_synth
DR PFAM; PF02547; Queuosine_synth
RA Slany RK, Bosl M, Crain PF, Kersten H.
RT A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine.
RL Biochemistry 32:7811-7817.
SE TIGR
GA hmmls
AL clustalw
DR HAMAP; MF_00113; 367 of 372 |
| Genome Property | GenProp0677: queuosine (Q-tRNA) biosynthesis from preQ0 (HMM) |
