Methionine--tRNA ligase

Details

Name
Methionine--tRNA ligase
Synonyms
  • 6.1.1.10
  • Methionyl-tRNA synthetase
  • MetRS
Gene Name
metG
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0003052|Methionine--tRNA ligase
MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIM
LKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFI
KNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSPTELIEPKSVVSG
ATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFG
FEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVY
FHSLFWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY
TAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLASELADPQLYK
TFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICSM
GINLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRIDMRQV
EALVEASKEEVKAAAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLR
LTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKD
IFLLSPDAGAKPGHQVK
Number of residues
677
Molecular Weight
76254.1
Theoretical pI
5.65
GO Classification
Functions
ATP binding / methionine-tRNA ligase activity / tRNA binding / zinc ion binding
Processes
methionyl-tRNA aminoacylation
Components
cytosol / membrane
General Function
Zinc ion 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0019136|Methionine--tRNA ligase (metG)
ATGACTCAAGTCGCGAAGAAAATTCTGGTGACGTGCGCACTGCCGTACGCTAACGGCTCA
ATCCACCTCGGCCATATGCTGGAGCACATCCAGGCTGATGTCTGGGTCCGTTACCAGCGA
ATGCGCGGCCACGAGGTCAACTTCATCTGCGCCGACGATGCCCACGGTACACCGATCATG
CTGAAAGCTCAGCAGCTTGGTATCACCCCGGAGCAGATGATTGGCGAAATGAGTCAGGAG
CATCAGACTGATTTCGCAGGCTTTAACATCAGCTATGACAACTATCACTCGACGCACAGC
GAAGAGAACCGCCAGTTGTCAGAACTTATCTACTCTCGCCTGAAAGAAAACGGTTTTATT
AAAAACCGCACCATCTCTCAGCTGTACGATCCGGAAAAAGGCATGTTCCTGCCGGACCGT
TTTGTGAAAGGCACCTGCCCGAAATGTAAATCCCCGGATCAATACGGCGATAACTGCGAA
GTCTGCGGCGCGACCTACAGCCCGACTGAACTGATCGAGCCGAAATCGGTGGTTTCTGGC
GCTACGCCGGTAATGCGTGATTCTGAACACTTCTTCTTTGATCTGCCCTCTTTCAGCGAA
ATGTTGCAGGCATGGACCCGCAGCGGTGCGTTGCAGGAGCAGGTGGCAAATAAAATGCAG
GAGTGGTTTGAATCTGGCCTGCAACAGTGGGATATCTCCCGCGACGCCCCTTACTTCGGT
TTTGAAATTCCGAACGCGCCGGGCAAATATTTCTACGTCTGGCTGGACGCACCGATTGGC
TACATGGGTTCTTTCAAGAATCTGTGCGACAAGCGCGGCGACAGCGTAAGCTTCGATGAA
TACTGGAAGAAAGACTCCACCGCCGAGCTGTACCACTTCATCGGTAAAGATATTGTTTAC
TTCCACAGCCTGTTCTGGCCTGCCATGCTGGAAGGCAGCAACTTCCGCAAGCCGTCCAAC
CTGTTTGTTCATGGCTATGTGACGGTGAACGGCGCAAAGATGTCCAAGTCTCGCGGCACC
TTTATTAAAGCCAGCACCTGGCTGAATCATTTTGACGCAGACAGCCTGCGTTACTACTAC
ACTGCGAAACTCTCTTCGCGCATTGATGATATCGATCTCAACCTGGAAGATTTCGTTCAG
CGTGTGAATGCCGATATCGTTAACAAAGTGGTTAACCTGGCCTCCCGTAATGCGGGCTTT
ATCAACAAGCGTTTTGACGGCGTGCTGGCAAGCGAACTGGCTGACCCGCAGTTGTACAAA
ACCTTCACTGATGCCGCTGAAGTGATTGGTGAAGCGTGGGAAAGCCGTGAATTTGGTAAA
GCCGTGCGCGAAATCATGGCGCTGGCTGATCTGGCTAACCGCTATGTCGATGAACAGGCT
CCGTGGGTGGTGGCGAAACAGGAAGGCCGCGATGCCGACCTGCAGGCAATTTGCTCAATG
GGCATCAACCTGTTCCGCGTGCTGATGACTTACCTGAAGCCGGTACTGCCGAAACTGACC
GAGCGTGCAGAAGCATTCCTCAATACGGAACTGACCTGGGATGGTATCCAGCAACCGCTG
CTGGGCCACAAAGTGAATCCGTTCAAGGCGCTGTATAACCGCATCGATATGAGGCAGGTT
GAAGCACTGGTGGAAGCCTCTAAAGAAGAAGTAAAAGCCGCTGCCGCGCCGGTAACTGGC
CCGCTGGCAGATGATCCGATTCAGGAAACCATCACCTTTGACGACTTCGCTAAAGTTGAC
CTGCGCGTGGCGCTGATTGAAAACGCAGAGTTTGTTGAAGGTTCTGACAAACTGCTGCGC
CTGACGCTGGATCTCGGCGGTGAAAAACGCAATGTCTTCTCCGGTATTCGTTCTGCTTAC
CCGGATCCGCAGGCACTGATTGGTCGTCACACCATTATGGTGGCTAACCTGGCACCACGT
AAAATGCGCTTCGGTATCTCTGAAGGCATGGTGATGGCTGCCGGTCCTGGCGGGAAAGAT
ATTTTCCTGCTAAGCCCGGATGCCGGTGCTAAACCGGGTCATCAGGTGAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00959
UniProtKB Entry NameSYM_ECOLI
GenBank Protein ID146829
GenBank Gene IDK02671
General References
  1. Dardel F, Fayat G, Blanquet S: Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene. J Bacteriol. 1984 Dec;160(3):1115-22. [Article]
  2. Dardel F, Panvert M, Fayat G: Transcription and regulation of expression of the Escherichia coli methionyl-tRNA synthetase gene. Mol Gen Genet. 1990 Aug;223(1):121-33. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Barker DG, Ebel JP, Jakes R, Bruton CJ: Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment. Eur J Biochem. 1982 Oct;127(3):449-57. [Article]
  6. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  7. Zelwer C, Risler JL, Brunie S: Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5 A resolution. J Mol Biol. 1982 Feb 15;155(1):63-81. [Article]
  8. Brunie S, Zelwer C, Risler JL: Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP. J Mol Biol. 1990 Nov 20;216(2):411-24. [Article]
  9. Mechulam Y, Schmitt E, Maveyraud L, Zelwer C, Nureki O, Yokoyama S, Konno M, Blanquet S: Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features. J Mol Biol. 1999 Dec 17;294(5):1287-97. [Article]
  10. Serre L, Verdon G, Choinowski T, Hervouet N, Risler JL, Zelwer C: How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding. J Mol Biol. 2001 Mar 2;306(4):863-76. [Article]
  11. Fourmy D, Dardel F, Blanquet S: Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins. J Mol Biol. 1993 Jun 20;231(4):1078-89. [Article]
  12. Hountondji C, Schmitter JM, Beauvallet C, Blanquet S: 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. 1990 Sep 4;29(35):8190-8. [Article]
  13. Meinnel T, Mechulam Y, Dardel F, Schmitter JM, Hountondji C, Brunie S, Dessen P, Fayat G, Blanquet S: Methionyl-tRNA synthetase from E. coli--a review. Biochimie. 1990 Aug;72(8):625-32. [Article]
  14. Fourmy D, Mechulam Y, Brunie S, Blanquet S, Fayat G: Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase. FEBS Lett. 1991 Nov 4;292(1-2):259-63. [Article]
  15. Fourmy D, Meinnel T, Mechulam Y, Blanquet S: Mapping of the zinc binding domain of Escherichia coli methionyl-tRNA synthetase. J Mol Biol. 1993 Jun 20;231(4):1068-77. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02151Methionine PhosphonateexperimentalunknownDetails
DB022295'-O-[(L-methionyl)-sulphamoyl]adenosineexperimentalunknownDetails
DB03799TrifluoromethionineexperimentalunknownDetails
DB03816DifluoromethionineexperimentalunknownDetails
DB04015Methionine PhosphinateexperimentalunknownDetails