Methionyl-tRNA synthetase (P00959)

Identification
Name:Methionyl-tRNA synthetase
Synonyms:
  • Methionine--tRNA ligase
  • MetRS
Gene Name:metG
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Met)+1.0tRNA(Met) ↔ 1.0Thumb+1.0Thumb+1.0L-Methionyl-tRNA+1.0L-Methionyl-tRNA
1.0Adenosine triphosphate + 1.0L-Methionine + 1.0tRNA(Met) + 1.0tRNA(Met) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Methionyl-tRNA + 1.0L-Methionyl-tRNA
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0tRNA(Met) → 1.0Thumb+1.0Pyrophosphate+1.0L-methionyl-tRNA(Met)
1.0L-Methionine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Met) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-methionyl-tRNA(Met)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Met) → 1.0Thumb+1.0L-Methionyl-tRNA (Met)+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Methionine + 1.0tRNA(Met) → 1.0Adenosine monophosphate + 1.0L-Methionyl-tRNA (Met) + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Met) → 1.0Thumb+1.0Thumb+1.0L-methionyl-tRNA(Met)
1.0Adenosine triphosphate + 1.0L-Methionine + 1.0tRNA(Met) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-methionyl-tRNA(Met)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00696L-MethionineMetaboCard
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
methionine-tRNA ligase activity
nucleic acid binding
nucleoside binding
nucleotide binding
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
methionyl-tRNA aminoacylation
ncRNA metabolic process
RNA metabolic process
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b2114
Gene OrientationClockwise
Centisome Percentage:47.25
Left Sequence End2192322
Right Sequence End2194355
Gene Sequence:
>2034 bp
ATGACAGACCTTTCACACAGCAGGGAAAAGGACAAAATCAATCCGGTGGTGTTTTACACC
TCCGCCGGACTGATTTTGTTGTTTTCCCTGACAACGATCCTGTTTCGCGACTTCTCGGCC
CTGTGGATTGGCCGCACGCTGGACTGGGTTTCTAAAACCTTCGGTTGGTACTATCTGCTG
GCGGCAACGCTCTATATTGTCTTTGTGGTCTGTATCGCTTGTTCGCGTTTTGGTTCGGTG
AAGCTCGGGCCAGAACAATCCAAACCGGAATTCAGCCTGCTGAGTTGGGCGGCGATGCTG
TTTGCTGCCGGGATCGGTATCGACCTGATGTTCTTCTCCGTAGCCGAACCGGTAACGCAG
TATATGCAGCCGCCGGAAGGCGCGGGACAGACGATTGAGGCCGCGCGTCAGGCGATGGTC
TGGACGCTGTTTCACTACGGCTTAACCGGCTGGTCGATGTATGCGCTGATGGGCATGGCG
CTCGGATACTTTAGCTATCGTTATAATTTGCCGCTCACCATCCGCTCGGCGCTGTACCCG
ATCTTCGGTAAACGGATTAACGGGCCGATAGGTCACTCAGTGGATATTGCAGCGGTGATC
GGCACTATCTTCGGTATTGCCACTACGCTCGGTATCGGTGTGGTGCAGCTTAACTATGGC
TTGAGCGTACTGTTTGATATTCCCGATTCGATGGCGGCGAAAGCGGCACTGATCGCCTTG
TCGGTGATAATCGCCACGATCTCTGTCACCTCCGGTGTCGATAAGGGCATTCGCGTGTTA
TCGGAGCTTAATGTCGCGCTGGCGCTGGGATTGATCCTGTTCGTATTGTTTATGGGCGAC
ACTTCGTTCCTGCTTAATGCACTGGTGCTGAATGTTGGCGACTATGTGAATCGCTTTATG
GGCATGACGCTCAACAGTTTTGCCTTCGACCGTCCGGTTGAGTGGATGAATAACTGGACG
CTCTTCTTCTGGGCATGGTGGGTGGCATGGTCGCCGTTTGTCGGCTTGTTCCTGGCGCGT
ATCTCGCGTGGGCGTACCATTCGCCAGTTCGTGCTGGGCACGTTGATTATTCCGTTTACC
TTCACGCTGTTATGGCTCTCGGTGTTCGGCAATAGCGCGCTGTATGAAATCATCCACGGC
GGCGCGGCATTTGCCGAGGAAGCGATGGTCCATCCGGAGCGCGGCTTCTACAGCCTGCTG
GCGCAGTATCCGGCGTTTACCTTTAGCGCCTCCGTCGCCACCATTACTGGCCTGCTGTTT
TATGTGACCTCGGCGGACTCCGGGGCGCTGGTGCTGGGGAATTTCACCTCGCAGCTTAAA
GATATCAACAGCGACGCCCCCGGCTGGCTGCGCGTCTTCTGGTCGGTGGCGATTGGCCTG
CTGACGCTCGGCATGCTGATGACTAACGGGATATCCGCGCTGCAAAACACCACGGTGATT
ATGGGGCTGCCGTTCAGCTTTGTGATCTTCTTCGTGATGGCGGGGTTGTATAAATCTCTG
AAGGTAGAAGATTACCGCCGTGAAAGTGCCAACCGCGATACCGCACCGCGACCGCTGGGG
CTTCAGGATCGCCTGAGCTGGAAAAAACGTCTCTCGCGCCTGATGAATTATCCGGGCACG
CGTTACACTAAACAGATGATGGAGACGGTCTGTTACCCGGCAATGGAAGAAGTGGCGCAG
GAGTTGCGGTTGCGCGGCGCGTACGTGGAGCTAAAAAGCCTGCCACCGGAAGAGGGACAG
CAGTTGGGTCATCTGGATTTGTTGGTGCATATGGGCGAAGAGCAAAACTTTGTCTATCAG
ATTTGGCCGCAGCAATATTCGGTGCCGGGCTTTACCTACCGCGCACGCAGCGGTAAATCG
ACCTACTACCGGCTGGAAACCTTCCTGTTAGAAGGCAGCCAGGGCAACGACCTGATGGAC
TACAGCAAAGAGCAGGTGATCACCGATATTCTTGACCAGTACGAGCGGCACCTTAACTTT
ATTCATCTCCATCGTGAAGCGCCGGGCCATAGCGTGATGTTCCCGGACGCGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:677
Protein Molecular Weight:76254
Protein Theoretical pI:6
PDB File:1PG0
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Methionyl-tRNA synthetase
MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIM
LKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFI
KNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSPTELIEPKSVVSG
ATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFG
FEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVY
FHSLFWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY
TAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLASELADPQLYK
TFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICSM
GINLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRIDMRQV
EALVEASKEEVKAAAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLR
LTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKD
IFLLSPDAGAKPGHQVK
References
External Links:
ResourceLink
Uniprot ID:P00959
Uniprot Name:SYM_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674457
PDB ID:1PG0
Ecogene ID:EG10586
Ecocyc:EG10586
ColiBase:b2114
Kegg Gene:b2114
EchoBASE ID:EB0581
CCDB:SYM_ECOLI
BacMap:16130052
General Reference:
  • Barker, D. G., Ebel, J. P., Jakes, R., Bruton, C. J. (1982). "Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment." Eur J Biochem 127:449-457. Pubmed: 6756915
  • 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
  • Brunie, S., Zelwer, C., Risler, J. L. (1990). "Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP." J Mol Biol 216:411-424. Pubmed: 2254937
  • Dardel, F., Fayat, G., Blanquet, S. (1984). "Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene." J Bacteriol 160:1115-1122. Pubmed: 6094501
  • Dardel, F., Panvert, M., Fayat, G. (1990). "Transcription and regulation of expression of the Escherichia coli methionyl-tRNA synthetase gene." Mol Gen Genet 223:121-133. Pubmed: 2259334
  • Fourmy, D., Dardel, F., Blanquet, S. (1993). "Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins." J Mol Biol 231:1078-1089. Pubmed: 8515466
  • Fourmy, D., Mechulam, Y., Brunie, S., Blanquet, S., Fayat, G. (1991). "Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase." FEBS Lett 292:259-263. Pubmed: 1959615
  • Fourmy, D., Meinnel, T., Mechulam, Y., Blanquet, S. (1993). "Mapping of the zinc binding domain of Escherichia coli methionyl-tRNA synthetase." J Mol Biol 231:1068-1077. Pubmed: 8515465
  • 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
  • Hountondji, C., Schmitter, J. M., Beauvallet, C., Blanquet, S. (1990). "Mapping of the active site of Escherichia coli methionyl-tRNA synthetase: identification of amino acid residues labeled by periodate-oxidized tRNA(fMet) molecules having modified lengths at the 3'-acceptor end." Biochemistry 29:8190-8198. Pubmed: 1702021
  • Mechulam, Y., Schmitt, E., Maveyraud, L., Zelwer, C., Nureki, O., Yokoyama, S., Konno, M., Blanquet, S. (1999). "Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features." J Mol Biol 294:1287-1297. Pubmed: 10600385
  • Meinnel, T., Mechulam, Y., Dardel, F., Schmitter, J. M., Hountondji, C., Brunie, S., Dessen, P., Fayat, G., Blanquet, S. (1990). "Methionyl-tRNA synthetase from E. coli--a review." Biochimie 72:625-632. Pubmed: 2126467
  • Serre, L., Verdon, G., Choinowski, T., Hervouet, N., Risler, J. L., Zelwer, C. (2001). "How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding." J Mol Biol 306:863-876. Pubmed: 11243794
  • Zelwer, C., Risler, J. L., Brunie, S. (1982). "Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5 A resolution." J Mol Biol 155:63-81. Pubmed: 7042987