Identification |
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Name: | Glycyl-tRNA synthetase beta subunit |
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Synonyms: | - Glycine--tRNA ligase beta subunit
- GlyRS
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Gene Name: | glyS |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in arginine-tRNA ligase activity |
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Specific Function: | ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly) |
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Cellular Location: | Cytoplasm |
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SMPDB Pathways: | |
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KEGG Pathways: | - Aminoacyl-tRNA biosynthesis ec00970
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KEGG Reactions: | |
1.0 | + | 1.0 | + | 1.0tRNA(Gly) | + | 1.0tRNA(Gly) | ↔ | 1.0 | + | 1.0Glycyl-tRNA(Gly) | + | 1.0 | + | 1.0Glycyl-tRNA(Gly) |
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1.0 | + | 1.0 | + | 1.0tRNA(Gly) | ↔ | 1.0 | + | 1.0 | + | 1.0Glycyl-tRNA(Gly) |
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SMPDB Reactions: | |
1.0 | + | 1.0 | + | 1.0 | + | 1.0tRNA(gly) | → | 1.0 | + | 1.0Pyrophosphate | + | 1.0Glycyl-tRNA(Gly) |
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Metabolites: | |
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GO Classification: | Component |
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cell part | cytoplasm | intracellular part | Function |
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adenyl nucleotide binding | adenyl ribonucleotide binding | aminoacyl-tRNA ligase activity | arginine-tRNA ligase activity | ATP binding | binding | catalytic activity | glycine-tRNA ligase activity | ligase activity | ligase activity, forming aminoacyl-tRNA and related compounds | ligase activity, forming carbon-oxygen bonds | nucleoside binding | nucleotide binding | purine nucleoside binding | Process |
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arginyl-tRNA aminoacylation | biosynthetic process | cellular macromolecule biosynthetic process | cellular macromolecule metabolic process | glycyl-tRNA aminoacylation | macromolecule biosynthetic process | macromolecule metabolic process | metabolic process | ncRNA metabolic process | RNA metabolic process | translation | tRNA aminoacylation | tRNA aminoacylation for protein translation | tRNA metabolic process |
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Gene Properties |
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Blattner: | b3559 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 80.19 |
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Left Sequence End | 3720351 |
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Right Sequence End | 3722420 |
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Gene Sequence: | >2070 bp
ATGTCTGAGAAAACTTTTCTGGTGGAAATCGGCACTGAAGAGCTGCCACCAAAAGCACTG
CGCAGCCTGGCTGAGTCCTTTGCTGCGAACTTTACTGCGGAGCTGGATAACGCTGGCCTC
GCACACGGCACCGTTCAATGGTTTGCTGCTCCGCGTCGTCTGGCGCTGAAAGTAGCTAAC
CTGGCGGAAGCGCAACCGGATCGTGAAATCGAAAAACGCGGCCCGGCGATTGCCCAGGCG
TTCGACGCTGAAGGCAAACCGAGCAAAGCGGCAGAAGGTTGGGCGCGTGGTTGCGGTATT
ACCGTTGACCAGGCTGAGCGTCTGACTACCGATAAAGGCGAATGGCTGCTGTATCGCGCC
CATGTGAAGGGCGAAAGCACCGAAGCACTGCTGCCGAATATGGTTGCGACTTCTCTGGCG
AAACTGCCGATCCCGAAACTGATGCGTTGGGGCGCAAGCGACGTGCACTTCGTGCGTCCG
GTGCACACCGTGACCCTGCTGCTGGGCGACAAAGTCATTCCGGCAACCATTCTGGGCATT
CAGTCCGATCGCGTGATTCGCGGCCACCGCTTTATGGGCGAGCCGGAATTCACCATCGAT
AACGCCGATCAGTATCCGGAAATTCTGCGTGAGCGTGGGAAAGTCATCGCCGATTACGAA
GAACGTAAGGCGAAGATTAAAGCCGATGCCGAAGAAGCAGCGCGTAAGATTGGCGGTAAC
GCTGACTTAAGCGAAAGCCTGCTGGAAGAAGTGGCTTCGCTGGTGGAGTGGCCGGTCGTT
CTGACCGCAAAATTCGAAGAGAAATTCCTCGCGGTGCCGGCTGAAGCGCTGGTTTACACC
ATGAAAGGTGACCAGAAATACTTCCCGGTGTATGCGAACGACGGCAAACTGCTGCCGAAC
TTTATCTTCGTTGCCAACATCGAATCGAAAGATCCGCAGCAGATTATCTCCGGTAACGAG
AAAGTCGTTCGTCCGCGTCTGGCGGATGCCGAGTTCTTCTTCAACACCGACCGTAAAAAA
CGTCTTGAAGATAACCTGCCGCGCCTGCAAACCGTGTTGTTCCAGCAACAGTTGGGGACG
CTGCGCGACAAAACTGACCGCATCCAGGCGCTGGCTGGCTGGATTGCTGAACAGATTGGC
GCTGACGTTAACCACGCTACCCGTGCGGGTCTGCTGTCTAAGTGCGACCTGATGACCAAC
ATGGTCTTCGAGTTCACCGACACCCAGGGCGTTATGGGGATGCACTATGCGCGTCACGAT
GGCGAAGCGGAAGATGTCGCGGTGGCGCTGAATGAGCAGTATCAGCCGCGTTTTGCTGGT
GATGACCTGCCGTCCAACCCAGTAGCTTGTGCGCTGGCGATTGCTGACAAGATGGATACC
CTGGCGGGTATCTTCGGTATCGGTCAGCATCCGAAAGGCGACAAAGACCCGTTTGCGCTG
CGTCGTGCCGCGCTTGGCGTGCTGCGAATTATCGTTGAGAAGAACCTCAACCTTGATCTG
CAAACGCTGACCGAAGAAGCGGTGCGTCTGTATGGCGATAAGCTGACTAATGCCAACGTA
GTTGATGATGTTATCGACTTTATGCTCGGTCGCTTCCGCGCCTGGTATCAGGACGAAGGT
TATACCGTTGACACCATCCAGGCGGTACTGGCGCGTCGTCCGACTCGTCCGGCTGATTTC
GATGCCCGTATGAAAGCGGTATCGCATTTCCGTACCCTGGATGCAGCTGCTGCACTGGCG
GCGGCGAACAAACGTGTATCTAACATTCTGGCGAAATCTGACGAAGTGCTGAGCGACCGC
GTGAATGCCTCTACCCTGAAAGAGCCGGAAGAAATTAAACTGGCGATGCAGGTTGTGGTG
CTACGTGACAAGCTGGAGCCGTACTTTACGGAAGGTCGTTACCAGGATGCGCTGGTCGAA
CTGGCTGAGCTGCGTGAACCGGTTGATGCTTTCTTCGATAAAGTGATGGTCATGGTTGAT
GACAAAGAATTGCGTATCAACCGTCTGACCATGCTGGAGAAACTGCGCGAACTGTTCCTG
CGCGTTGCGGATATTTCGCTGTTGCAATAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 689 |
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Protein Molecular Weight: | 76812 |
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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: | >Glycyl-tRNA synthetase beta subunit
MSEKTFLVEIGTEELPPKALRSLAESFAANFTAELDNAGLAHGTVQWFAAPRRLALKVAN
LAEAQPDREIEKRGPAIAQAFDAEGKPSKAAEGWARGCGITVDQAERLTTDKGEWLLYRA
HVKGESTEALLPNMVATSLAKLPIPKLMRWGASDVHFVRPVHTVTLLLGDKVIPATILGI
QSDRVIRGHRFMGEPEFTIDNADQYPEILRERGKVIADYEERKAKIKADAEEAARKIGGN
ADLSESLLEEVASLVEWPVVLTAKFEEKFLAVPAEALVYTMKGDQKYFPVYANDGKLLPN
FIFVANIESKDPQQIISGNEKVVRPRLADAEFFFNTDRKKRLEDNLPRLQTVLFQQQLGT
LRDKTDRIQALAGWIAEQIGADVNHATRAGLLSKCDLMTNMVFEFTDTQGVMGMHYARHD
GEAEDVAVALNEQYQPRFAGDDLPSNPVACALAIADKMDTLAGIFGIGQHPKGDKDPFAL
RRAALGVLRIIVEKNLNLDLQTLTEEAVRLYGDKLTNANVVDDVIDFMLGRFRAWYQDEG
YTVDTIQAVLARRPTRPADFDARMKAVSHFRTLDAAAALAAANKRVSNILAKSDEVLSDR
VNASTLKEPEEIKLAMQVVVLRDKLEPYFTEGRYQDALVELAELREPVDAFFDKVMVMVD
DKELRINRLTMLEKLRELFLRVADISLLQ |
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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
- Keng, T., Webster, T. A., Sauer, R. T., Schimmel, P. (1982). "Gene for Escherichia coli glycyl-tRNA synthetase has tandem subunit coding regions in the same reading frame." J Biol Chem 257:12503-12508. Pubmed: 6290471
- Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
- Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620
- Webster, T. A., Gibson, B. W., Keng, T., Biemann, K., Schimmel, P. (1983). "Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase." J Biol Chem 258:10637-10641. Pubmed: 6309809
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