Seryl-tRNA synthetase (P0A8L1)

Identification
Name:Seryl-tRNA synthetase
Synonyms:
  • Serine--tRNA ligase
  • SerRS
  • Seryl-tRNA(Ser/Sec) synthetase
Gene Name:serS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Ser)+1.0tRNA(Ser) ↔ 1.0Thumb+1.0Thumb+1.0L-Seryl-tRNA(Ser)+1.0L-Seryl-tRNA(Ser)
1.0Adenosine triphosphate + 1.0L-Serine + 1.0tRNA(Ser) + 1.0tRNA(Ser) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Seryl-tRNA(Ser) + 1.0L-Seryl-tRNA(Ser)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Ser) ↔ 1.0Thumb+1.0Thumb+1.0L-Seryl-tRNA(Ser)
1.0Adenosine triphosphate + 1.0L-Serine + 1.0tRNA(Ser) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Seryl-tRNA(Ser)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Sec) ↔ 1.0Thumb+1.0Thumb+1.0L-Seryl-tRNA(Sec)
1.0Adenosine triphosphate + 1.0L-Serine + 1.0tRNA(Sec) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Seryl-tRNA(Sec)
ReactionCard
SMPDB Reactions:
1.0L-Serine+1.0Thumb+1.0Thumb+1.0tRNA(Ser)+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0L-Seryl-tRNA(Ser)
1.0L-Serine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Ser) + 1.0L-Serine → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Seryl-tRNA(Ser)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(SeCys) → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Serine + 1.0tRNA(SeCys) → 1.0Adenosine monophosphate + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Ser) → 1.0Thumb+1.0Thumb+1.0L-seryl-tRNA(Ser)
1.0Adenosine triphosphate + 1.0L-Serine + 1.0tRNA(Ser) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-seryl-tRNA(Ser)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Sec) → 1.0Thumb+1.0Thumb+1.0L-seryl-tRNA(Sec)
1.0Adenosine triphosphate + 1.0L-Serine + 1.0tRNA(Sec) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-seryl-tRNA(Sec)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00187L-SerineMetaboCard
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
nucleoside binding
nucleotide binding
purine nucleoside binding
serine-tRNA ligase activity
Process
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
macromolecule biosynthetic process
macromolecule metabolic process
metabolic process
ncRNA metabolic process
RNA metabolic process
seryl-tRNA aminoacylation
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b0893
Gene OrientationClockwise
Centisome Percentage:20.23
Left Sequence End938651
Right Sequence End939943
Gene Sequence:
>1293 bp
ATGATGAACACGGAAGGTAATAACGGTAACAAACCTCTCGGTCTATGGAACGTCGTTTCC
ATCGGCATTGGGGCAATGGTGGGGGCGGGGATCTTCGCGCTGCTGGGGCAGGCTGCATTG
CTAATGGAAGCCTCGACCTGGGTCGCCTTTGCTTTTGGCGGTATTGTGGCGATGTTTTCC
GGTTATGCCTATGCGCGTCTGGGGGCGAGCTATCCCAGCAATGGCGGCATTATCGACTTC
TTTCGTCGCGGATTAGGCAACGGCGTCTTTTCGCTGGCGCTCTCGTTACTGTACCTGTTG
ACGCTGGCGGTGAGCATCGCCATGGTCGCCCGTGCTTTTGGCGCTTATGCCGTGCAGTTT
TTGCATGAAGGCAGCCAGGAGGAGCACCTTATTTTGCTCTACGCGTTGGGGATCATTGCG
GTGATGACGCTTTTCAACTCCTTAAGCAACCATGCGGTAGGGCGGCTGGAAGTGATCCTC
GTCGGCATTAAAATGATGATCCTGTTATTGCTGATTATTGCCGGTGTCTGGTCGCTGCAA
CCGGCGCATATTTCCGTCTCTGCGCCCCCCAGCTCCGGTGCGTTCTTCTCCTGTATTGGG
ATAACTTTCCTTGCCTATGCGGGCTTTGGCATGATGGCGAACGCGGCGGATAAAGTGAAA
GATCCGCAGGTCATTATGCCACGGGCGTTTCTGGTGGCGATTGGCGTTACCACGTTGCTT
TATATCTCGCTGGCACTGGTTTTGCTTAGCGATGTATCGGCATTAGAGTTAGAAAAATAT
GCCGATACCGCCGTAGCGCAGGCTGCTTCTCCGCTGCTCGGGCATGTGGGTTATGTGATC
GTCGTCATCGGCGCTTTACTGGCGACGGCTTCAGCCATTAACGCGAACCTGTTCGCCGTG
TTTAACATCATGGACAACATGGGCAGCGAACGCGAACTGCCGAAGCTAATGAATAAATCC
CTGTGGCGGCAGAGTACCTGGGGCAACATTATTGTCGTGGTGTTGATTATGCTGATGACG
GCGGCACTGAATTTAGGCTCACTCGCCAGCGTTGCCAGCGCCACCTTTTTGATTTGCTAC
CTGGCGGTGTTTGTGGTGGCGATCCGCCTGCGTCATGATATTCACGCCTCGTTGCCGATT
CTTATCGTTGGTACGTTGGTGATGTTGTTGGTGATCGTTGGCTTTATCTACAGTCTGTGG
TCCCAGGGTAGCCGTGCGTTGATATGGATTATTGGCTCACTCTTACTCAGCCTTATTGTG
GCAATGGTCATGAAGCGCAATAAAACCGTATAA
Protein Properties
Pfam Domain Function:
Protein Residues:430
Protein Molecular Weight:48414
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Seryl-tRNA synthetase
MLDPNLLRNEPDAVAEKLARRGFKLDVDKLGALEERRKVLQVKTENLQAERNSRSKSIGQ
AKARGEDIEPLRLEVNKLGEELDAAKAELDALQAEIRDIALTIPNLPADEVPVGKDENDN
VEVSRWGTPREFDFEVRDHVTLGEMHSGLDFAAAVKLTGSRFVVMKGQIARMHRALSQFM
LDLHTEQHGYSENYVPYLVNQDTLYGTGQLPKFAGDLFHTRPLEEEADTSNYALIPTAEV
PLTNLVRGEIIDEDDLPIKMTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVEMVQIVRPED
SMAALEEMTGHAEKVLQLLGLPYRKIILCTGDMGFGACKTYDLEVWIPAQNTYREISSCS
NVWDFQARRMQARCRSKSDKKTRLVHTLNGSGLAVGRTLVAVMENYQQADGRIEVPEVLR
PYMNGLEYIG
References
External Links:
ResourceLink
Uniprot ID:P0A8L1
Uniprot Name:SYS_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674625
Ecogene ID:EG10947
Ecocyc:EG10947
ColiBase:b0893
Kegg Gene:b0893
EchoBASE ID:EB0940
CCDB:SYS_ECOLI
BacMap:16128860
General Reference:
  • Bilous, P. T., Cole, S. T., Anderson, W. F., Weiner, J. H. (1988). "Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli." Mol Microbiol 2:785-795. Pubmed: 3062312
  • 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
  • Borel, F., Vincent, C., Leberman, R., Hartlein, M. (1994). "Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity." Nucleic Acids Res 22:2963-2969. Pubmed: 8065908
  • Cusack, S., Berthet-Colominas, C., Hartlein, M., Nassar, N., Leberman, R. (1990). "A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A." Nature 347:249-255. Pubmed: 2205803
  • Hartlein, M., Madern, D., Leberman, R. (1987). "Cloning and characterization of the gene for Escherichia coli seryl-tRNA synthetase." Nucleic Acids Res 15:1005-1017. Pubmed: 3029694
  • 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
  • Leberman, R., Hartlein, M., Cusack, S. (1991). "Escherichia coli seryl-tRNA synthetase: the structure of a class 2 aminoacyl-tRNA synthetase." Biochim Biophys Acta 1089:287-298. Pubmed: 1859832
  • Leinfelder, W., Zehelein, E., Mandrand-Berthelot, M. A., Bock, A. (1988). "Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine." Nature 331:723-725. Pubmed: 2963963
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Price, S., Cusack, S., Borel, F., Berthet-Colominas, C., Leberman, R. (1993). "Crystallization of the seryl-tRNA synthetase:tRNAS(ser) complex of Escherichia coli." FEBS Lett 324:167-170. Pubmed: 8508916
  • Vincent, C., Borel, F., Willison, J. C., Leberman, R., Hartlein, M. (1995). "Seryl-tRNA synthetase from Escherichia coli: functional evidence for cross-dimer tRNA binding during aminoacylation." Nucleic Acids Res 23:1113-1118. Pubmed: 7537870