Prolyl-tRNA synthetase (P16659)

Identification
Name:Prolyl-tRNA synthetase
Synonyms:
  • Global RNA synthesis factor
  • Proline--tRNA ligase
  • ProRS
Gene Name:proS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction:proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). Misacylated Cys-tRNA(Pro) is not edited by ProRS, but instead may be edited in trans by ybaK
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Pro)+1.0tRNA(Pro) ↔ 1.0Thumb+1.0Thumb+1.0L-Prolyl-tRNA(Pro)+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Proline + 1.0tRNA(Pro) + 1.0tRNA(Pro) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Prolyl-tRNA(Pro) + 1.0L-Prolyl-tRNA(Pro)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Pro) ↔ 1.0Thumb+1.0Thumb+1.0L-Prolyl-tRNA(Pro)
1.0Adenosine triphosphate + 1.0L-Proline + 1.0tRNA(Pro) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Prolyl-tRNA(Pro)
ReactionCard
SMPDB Reactions:
1.0L-Proline+1.0Thumb+1.0Thumb+1.0tRNA(Pro)+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0L-prolyl-tRNA(Pro)
1.0L-Proline + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Pro) + 1.0L-Proline → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-prolyl-tRNA(Pro)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Pro) → 1.0Thumb+1.0Thumb+1.0L-prolyl-tRNA(Pro)
1.0Adenosine triphosphate + 1.0L-Proline + 1.0tRNA(Pro) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-prolyl-tRNA(Pro)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00162L-ProlineMetaboCard
ECMDB23800L-Prolyl-tRNA(Pro)MetaboCard
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
proline-tRNA ligase activity
purine nucleoside binding
Process
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
macromolecule biosynthetic process
macromolecule metabolic process
metabolic process
ncRNA metabolic process
prolyl-tRNA aminoacylation
RNA metabolic process
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b0194
Gene OrientationCounterclockwise
Centisome Percentage:4.68
Left Sequence End217057
Right Sequence End218775
Gene Sequence:
>1719 bp
ATGCGTACTAGCCAATACCTGCTCTCCACTCTCAAGGAGACACCTGCCGACGCCGAGGTG
ATCAGCCATCAGCTGATGCTGCGCGCCGGGATGATCCGCAAGCTGGCCTCCGGGTTATAT
ACCTGGCTGCCGACCGGCGTGCGCGTTCTGAAAAAAGTCGAAAACATCGTGCGTGAAGAG
ATGAACAACGCCGGTGCGATCGAGGTGTCGATGCCGGTGGTTCAGCCAGCCGATTTGTGG
CAAGAGAGTGGTCGTTGGGAACAGTACGGTCCGGAACTGCTGCGTTTTGTTGACCGTGGC
GAGCGTCCGTTCGTACTCGGCCCAACTCATGAAGAAGTTATCACTGACCTGATTCGTAAC
GAGCTTAGCTCTTACAAACAGCTGCCGCTGAACTTCTATCAGATCCAGACCAAGTTCCGC
GACGAAGTGCGTCCGCGTTTCGGCGTCATGCGTTCCCGCGAATTCCTGATGAAAGATGCT
TACTCTTTCCATACTTCTCAGGAATCCCTGCAGGAAACCTACGATGCAATGTATGCGGCC
TACAGCAAAATCTTCAGCCGCATGGGGCTGGATTTCCGCGCCGTACAAGCCGACACCGGT
TCTATCGGCGGCAGCGCCTCTCACGAATTCCAGGTGCTGGCGCAGAGCGGTGAAGACGAT
GTGGTCTTCTCCGACACCTCTGACTATGCAGCGAACATTGAACTGGCAGAAGCTATCGCG
CCGAAAGAACCGCGCGCTGCTGCTACCCAGGAAATGACGCTGGTTGATACGCCGAACGCG
AAAACCATCGCGGAACTGGTTGAACAGTTCAATCTGCCGATTGAGAAAACGGTTAAGACT
CTGCTGGTTAAAGCGGTTGAAGGCAGCAGCTTCCCGCAGGTTGCGCTGCTGGTGCGCGGT
GATCACGAGCTGAACGAAGTTAAAGCAGAAAAACTGCCGCAGGTTGCAAGCCCGCTGACT
TTCGCGACCGAAGAAGAAATTCGTGCCGTGGTTAAAGCCGGTCCGGGTTCACTGGGTCCG
GTAAACATGCCGATTCCGGTGGTGATTGACCGTACCGTTGCGGCGATGAGTGATTTCGCT
GCTGGTGCTAACATCGATGGTAAACACTACTTCGGCATCAACTGGGATCGCGATGTCGCT
ACCCCGGAAGTTGCAGATATCCGTAACGTGGTGGCTGGCGATCCAAGCCCGGATGGCCAG
GGTAGGCTGCTGATCAAACGTGGTATCGAAGTTGGTCACATCTTCCAGCTGGGTACCAAG
TACTCCGAAGCACTGAAAGCCTCCGTACAGGGTGAAGATGGCCGTAACCAAATCCTGACG
ATGGGTTGCTACGGTATCGGGGTAACGCGTGTGGTAGCTGCGGCGATTGAGCAGAACTAC
GACGAACGAGGCATCGTATGGCCTGACGCTATCGCGCCGTTCCAGGTGGCGATTCTGCCG
ATGAACATGCACAAATCCTTCCGCGTACAAGAGCTTGCTGAGAAACTGTACAGCGAACTG
CGTGCACAAGGTATCGAAGTGCTGCTGGATGACCGCAAAGAGCGTCCGGGCGTGATGTTT
GCTGATATGGAACTGATCGGTATTCCGCACACTATTGTGCTGGGCGACCGTAACCTCGAC
AACGACGATATCGAATATAAATATCGTCGCAACGGCGAGAAACAGTTAATTAAGACTGGT
GACATCGTCGAATATCTGGTGAAACAGATTAAAGGCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:572
Protein Molecular Weight:63692
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Prolyl-tRNA synthetase
MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREE
MNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLIRN
ELSSYKQLPLNFYQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTSQESLQETYDAMYAA
YSKIFSRMGLDFRAVQADTGSIGGSASHEFQVLAQSGEDDVVFSDTSDYAANIELAEAIA
PKEPRAAATQEMTLVDTPNAKTIAELVEQFNLPIEKTVKTLLVKAVEGSSFPQVALLVRG
DHELNEVKAEKLPQVASPLTFATEEEIRAVVKAGPGSLGPVNMPIPVVIDRTVAAMSDFA
AGANIDGKHYFGINWDRDVATPEVADIRNVVAGDPSPDGQGRLLIKRGIEVGHIFQLGTK
YSEALKASVQGEDGRNQILTMGCYGIGVTRVVAAAIEQNYDERGIVWPDAIAPFQVAILP
MNMHKSFRVQELAEKLYSELRAQGIEVLLDDRKERPGVMFADMELIGIPHTIVLGDRNLD
NDDIEYKYRRNGEKQLIKTGDIVEYLVKQIKG
References
External Links:
ResourceLink
Uniprot ID:P16659
Uniprot Name:SYP_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674379
Ecogene ID:EG10770
Ecocyc:EG10770
ColiBase:b0194
Kegg Gene:b0194
EchoBASE ID:EB0763
CCDB:SYP_ECOLI
BacMap:16128187
General Reference:
  • Ahel, I., Stathopoulos, C., Ambrogelly, A., Sauerwald, A., Toogood, H., Hartsch, T., Soll, D. (2002). "Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases." J Biol Chem 277:34743-34748. Pubmed: 12130657
  • Beuning, P. J., Musier-Forsyth, K. (2000). "Hydrolytic editing by a class II aminoacyl-tRNA synthetase." Proc Natl Acad Sci U S A 97:8916-8920. Pubmed: 10922054
  • Beuning, P. J., Musier-Forsyth, K. (2001). "Species-specific differences in amino acid editing by class II prolyl-tRNA synthetase." J Biol Chem 276:30779-30785. Pubmed: 11408489
  • 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
  • Eriani, G., Delarue, M., Poch, O., Gangloff, J., Moras, D. (1990). "Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs." Nature 347:203-206. Pubmed: 2203971
  • 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
  • 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
  • Wong, F. C., Beuning, P. J., Nagan, M., Shiba, K., Musier-Forsyth, K. (2002). "Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing." Biochemistry 41:7108-7115. Pubmed: 12033945
  • Wong, F. C., Beuning, P. J., Silvers, C., Musier-Forsyth, K. (2003). "An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing." J Biol Chem 278:52857-52864. Pubmed: 14530268
  • Zhou, Z., Syvanen, M. (1990). "Identification and sequence of the drpA gene from Escherichia coli." J Bacteriol 172:281-286. Pubmed: 1688424