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
- FunctionsATP binding / methionine-tRNA ligase activity / tRNA binding / zinc ion bindingProcessesmethionyl-tRNA aminoacylationComponentscytosol / 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
Resource Link UniProtKB ID P00959 UniProtKB Entry Name SYM_ECOLI GenBank Protein ID 146829 GenBank Gene ID K02671 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB02151 Methionine Phosphonate experimental unknown Details DB02229 5'-O-[(L-methionyl)-sulphamoyl]adenosine experimental unknown Details DB03799 Trifluoromethionine experimental unknown Details DB03816 Difluoromethionine experimental unknown Details DB04015 Methionine Phosphinate experimental unknown Details