| Identification |
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| Name: | S-adenosylmethionine:tRNA ribosyltransferase-isomerase |
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| Synonyms: | - Queuosine biosynthesis protein queA
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| Gene Name: | queA |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Translation, ribosomal structure and biogenesis |
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| Specific Function: | Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA) |
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| Cellular Location: | Cytoplasm (Potential) |
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| SMPDB Pathways: | |
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| KEGG Pathways: | Not Available |
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| SMPDB Reactions: | |
1.07-aminomethyl-7-deazaguanosine34 in tRNA | + | 1.0S-adenosyl-L-methionine | → | 1.0 | + | 1.0 | + | 1.0 | + | 1.0 |
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| Metabolites: | |
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| GO Classification: | | Function |
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| catalytic activity | | isomerase activity | | transferase activity | | Process |
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| cellular macromolecule metabolic process | | macromolecule metabolic process | | metabolic process | | ncRNA metabolic process | | queuosine biosynthetic process | | RNA metabolic process | | tRNA metabolic process | | tRNA modification | | tRNA processing |
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| Gene Properties |
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| Blattner: | Not Available |
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| Gene Orientation | Not Available |
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| Centisome Percentage: | Not Available |
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| Left Sequence End | Not Available |
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| Right Sequence End | Not Available |
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| Gene Sequence: | >1071 bp
ATGCGCGTTACCGATTTCTCCTTTGAATTGCCCGAATCCCTGATTGCCCACTATCCCATG
CCTGAACGCAGTAGCTGTCGTTTACTGTCGCTGGACGGGCCGACGGGCGCGCTGACGCAC
GGTACTTTCACCGATTTACTTGATAAGCTCAACCCCGGCGATCTTCTGGTTTTTAATAAT
ACCCGCGTGATCCCGGCGCGCCTGTTTGGGCGTAAAGCCAGCGGCGGCAAGATTGAAGTG
CTGGTTGAACGGATGCTCGACGACAAACGCATTCTTGCGCATATTCGCGCCTCGAAAGCG
CCAAAACCTGGCGCAGAACTGCTGCTGGGCGATGACGAAAGTATTAACGCAACAATGACC
GCGCGCCACGGCGCACTGTTTGAAGTCGAATTTAATGATGAACGCTCGGTGCTGGATATT
CTCAACAGCATCGGCCATATGCCGCTGCCGCCGTATATCGACCGTCCGGACGAAGACGCT
GACCGCGAACTTTATCAAACCGTTTATAGCGAAAAACCGGGCGCGGTTGCAGCCCCGACC
GCAGGTCTGCATTTTGACGAGCCTTTGCTGGAAAAATTGCGCGCCAAAGGCGTGGAGATG
GCGTTTGTGACGTTGCACGTTGGTGCGGGCACCTTCCAGCCGGTGCGCGTCGACACCATT
GAAGATCACATCATGCACTCGGAATACGCTGAAGTACCGCAGGATGTGGTAGACGCGGTA
CTGGCGGCGAAAGCGCGCGGTAACCGGGTGATTGCGGTTGGCACCACTTCAGTACGTTCG
CTGGAAAGCGCGGCTCAGGCAGCGAAAAACGATCTCATTGAACCGTTCTTCGACGATACC
CAAATCTTTATCTATCCGGGCTTCCAGTACAAAGTGGTCGATGCGCTGGTGACGAACTTC
CACTTGCCAGAGTCGACGCTGATTATGCTGGTTTCGGCCTTTGCCGGTTATCAACACACC
ATGAACGCCTATAAAGCAGCGGTAGAAGAGAAATATCGCTTTTTTAGTTACGGTGATGCG
ATGTTTATCACGTACAATCCGCAGGCAATTAATGAGCGCGTCGGGGAGTAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 356 |
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| Protein Molecular Weight: | 39430 |
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| Protein Theoretical pI: | 5 |
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| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >S-adenosylmethionine:tRNA ribosyltransferase-isomerase
MRVTDFSFELPESLIAHYPMPERSSCRLLSLDGPTGALTHGTFTDLLDKLNPGDLLVFNN
TRVIPARLFGRKASGGKIEVLVERMLDDKRILAHIRASKAPKPGAELLLGDDESINATMT
ARHGALFEVEFNDERSVLDILNSIGHMPLPPYIDRPDEDADRELYQTVYSEKPGAVAAPT
AGLHFDEPLLEKLRAKGVEMAFVTLHVGAGTFQPVRVDTIEDHIMHSEYAEVPQDVVDAV
LAAKARGNRVIAVGTTSVRSLESAAQAAKNDLIEPFFDDTQIFIYPGFQYKVVDALVTNF
HLPESTLIMLVSAFAGYQHTMNAYKAAVEEKYRFFSYGDAMFITYNPQAINERVGE |
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| References |
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| External Links: | |
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| General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Reuter, K., Slany, R., Ullrich, F., Kersten, H. (1991). "Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes." J Bacteriol 173:2256-2264. Pubmed: 1706703
- Slany, R. K., Bosl, M., Crain, P. F., Kersten, H. (1993). "A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine." Biochemistry 32:7811-7817. Pubmed: 8347586
- Slany, R. K., Bosl, M., Kersten, H. (1994). "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." Biochimie 76:389-393. Pubmed: 7849103
- Van Lanen, S. G., Iwata-Reuyl, D. (2003). "Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA)." Biochemistry 42:5312-5320. Pubmed: 12731872
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