Phenylalanyl-tRNA synthetase alpha chain (P08312)

Identification
Name:Phenylalanyl-tRNA synthetase alpha chain
Synonyms:
  • Phenylalanine--tRNA ligase alpha chain
  • PheRS
Gene Name:pheS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Phe)+1.0tRNA(Phe) ↔ 1.0Thumb+1.0L-Phenylalanyl-tRNA(Phe)+1.0Thumb+1.0L-Phenylalanyl-tRNA(Phe)
1.0Adenosine triphosphate + 1.0L-Phenylalanine + 1.0tRNA(Phe) + 1.0tRNA(Phe) ↔ 1.0Adenosine monophosphate + 1.0L-Phenylalanyl-tRNA(Phe) + 1.0Pyrophosphate + 1.0L-Phenylalanyl-tRNA(Phe)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Phe) ↔ 1.0Thumb+1.0Thumb+1.0L-Phenylalanyl-tRNA(Phe)
1.0Adenosine triphosphate + 1.0L-Phenylalanine + 1.0tRNA(Phe) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Phenylalanyl-tRNA(Phe)
ReactionCard
SMPDB Reactions:
1.0L-Phenylalanine+1.0Thumb+1.0Thumb+1.0tRNA(Phe)+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0L-phenylalanyl-tRNA(Phe)
1.0L-Phenylalanine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Phe) + 1.0L-Phenylalanine → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-phenylalanyl-tRNA(Phe)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Phe) → 1.0Thumb+1.0Thumb+1.0L-phenylalanyl-tRNA(Phe)
1.0Adenosine triphosphate + 1.0L-Phenylalanine + 1.0tRNA(Phe) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-phenylalanyl-tRNA(Phe)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00159L-PhenylalanineMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
aminoacyl-tRNA ligase activity
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-oxygen bonds
nucleic acid binding
nucleoside binding
nucleotide binding
phenylalanine-tRNA ligase activity
purine nucleoside binding
RNA binding
tRNA binding
Process
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
macromolecule biosynthetic process
macromolecule metabolic process
metabolic process
ncRNA metabolic process
phenylalanyl-tRNA aminoacylation
RNA metabolic process
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b1714
Gene OrientationCounterclockwise
Centisome Percentage:38.71
Left Sequence End1795983
Right Sequence End1796966
Gene Sequence:
>984 bp
GTGGAAGCGATTAAGGGATCGGACGTTAATGTCCCGGATGCAGTATTTGCCTGGATGCTG
GATGGTAGAGGCGGCGTTAAACCGCTGGAAAATACAGATGTGATTGATGAAGCGCATCCC
TGTTGGCTCCACCTTAATTATGTACACCATGATAGCGCCCAATGGCTGGCGACAACACCG
CTGCTTCCCAATAACGTACGTGATGCGCTGGCGGGCGAGAGCACGCGTCCCCGAGTCAGC
CGTCTCGGTGAAGGCACGCTGATTACATTGCGCTGTATAAACGGCAGCACCGATGAACGC
CCCGATCAACTGGTCGCCATGCGTGTATATATGGACGGGCGGTTAATTGTTTCGACCCGA
CAACGCAAAGTGCTGGCGCTGGACGATGTGGTGAGCGATCTGGAAGAGGGCACGGGTCCG
ACCGATTGCGGGGGATGGCTGGTGGATGTGTGCGATGCGTTGACCGATCATTCCAGTGAA
TTTATCGAGCAGCTGCACGATAAAATTATCGACCTTGAAGATAATCTCCTTGATCAGCAA
ATTCCACCGCGTGGATTCCTGGCTCTGCTGCGCAAACAATTAATTGTGATGCGTCGCTAT
ATGGCACCGCAACGTGATGTTTATGCTCGTCTTGCCAGTGAACGTTTGCCGTGGATGAGC
GATGACCAACGCCGTCGGATGCAGGATATTGCCGATCGCCTTGGGCGCGGCCTTGACGAA
ATCGACGCCTGTATAGCACGGACTGGCGTGATGGCGGATGAAATCGCTCAGGTGATGCAG
GAAAATTTAGCTCGTCGTACCTATACAATGTCGTTGATGGCAATGGTCTTTTTACCCAGT
ACCTTTCTGACCGGGTTATTTGGCGTCAACCTTGGTGGGATCCCTGGCGGCGGGTGGCAA
TTCGGATTTTCAATTTTTTGTATTCTGTTAGTTGTTCTTATTGGTGGTGTTGCTTTATGG
TTGCATCGTAGTAAATGGTTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:327
Protein Molecular Weight:36832
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phenylalanyl-tRNA synthetase alpha chain
MSHLAELVASAKAAISQASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVI
NEAKEQVQQALNARKAELESAALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFF
GELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDTTRLLRTQTSGVQIRTMKA
QQPPIRIIAPGRVYRNDYDQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDLQ
IRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGME
RLTMLRYGVTDLRSFFENDLRFLKQFK
References
External Links:
ResourceLink
Uniprot ID:P08312
Uniprot Name:SYFA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674915
Ecogene ID:EG10709
Ecocyc:EG10709
ColiBase:b1714
Kegg Gene:b1714
EchoBASE ID:EB0703
CCDB:SYFA_ECOLI
BacMap:16129670
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Fayat, G., Mayaux, J. F., Sacerdot, C., Fromant, M., Springer, M., Grunberg-Manago, M., Blanquet, S. (1983). "Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20." J Mol Biol 171:239-261. Pubmed: 6317865
  • 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
  • Kast, P., Hennecke, H. (1991). "Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations." J Mol Biol 222:99-124. Pubmed: 1942071
  • Kast, P., Keller, B., Hennecke, H. (1992). "Identification of the pheS5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37." J Bacteriol 174:1686-1689. Pubmed: 1537809
  • Kast, P., Wehrli, C., Hennecke, H. (1991). "Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA synthetases." FEBS Lett 293:160-163. Pubmed: 1959653
  • Mechulam, Y., Fayat, G., Blanquet, S. (1985). "Sequence of the Escherichia coli pheST operon and identification of the himA gene." J Bacteriol 163:787-791. Pubmed: 2991205