Methionyl-tRNA formyltransferase

Details

Name
Methionyl-tRNA formyltransferase
Synonyms
  • 2.1.2.9
  • yhdD
Gene Name
fmt
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012845|Methionyl-tRNA formyltransferase
MSESLRIIFAGTPDFAARHLDALLSSGHNVVGVFTQPDRPAGRGKKLMPSPVKVLAEEKG
LPVFQPVSLRPQENQQLVAELQADVMVVVAYGLILPKAVLEMPRLGCINVHGSLLPRWRG
AAPIQRSLWAGDAETGVTIMQMDVGLDTGDMLYKLSCPITAEDTSGTLYDKLAELGPQGL
ITTLKQLADGTAKPEVQDETLVTYAEKLSKEEARIDWSLSAAQLERCIRAFNPWPMSWLE
IEGQPVKVWKASVIDTATNAAPGTILEANKQGIQVATGDGILNLLSLQPAGKKAMSAQDL
LNSRREWFVPGNRLV
Number of residues
315
Molecular Weight
34168.16
Theoretical pI
5.45
GO Classification
Functions
methionyl-tRNA formyltransferase activity / methyltransferase activity
Processes
charged-tRNA amino acid modification / conversion of methionyl-tRNA to N-formyl-methionyl-tRNA / translational initiation
Components
cytosol
General Function
Methyltransferase activity
Specific Function
Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0012846|Methionyl-tRNA formyltransferase (fmt)
GTGTCAGAATCACTACGTATTATTTTTGCGGGTACACCTGACTTTGCAGCGCGTCATCTC
GACGCGCTGTTGTCTTCTGGTCATAACGTCGTTGGCGTGTTCACCCAGCCAGACCGACCG
GCAGGACGCGGTAAAAAACTGATGCCCAGCCCGGTTAAAGTTCTGGCTGAGGAAAAAGGT
CTGCCCGTTTTTCAACCTGTTTCCCTGCGTCCACAAGAAAACCAGCAACTGGTCGCCGAA
CTGCAGGCTGATGTTATGGTCGTCGTCGCCTATGGTTTAATTCTGCCGAAAGCAGTGCTG
GAGATGCCGCGTCTTGGCTGTATCAACGTTCATGGTTCACTGCTGCCACGCTGGCGCGGT
GCTGCACCAATCCAACGCTCACTATGGGCGGGTGATGCAGAAACTGGTGTGACCATTATG
CAAATGGATGTCGGTTTAGACACCGGTGATATGCTCTATAAGCTCTCCTGCCCGATTACT
GCAGAAGATACCAGTGGTACGCTGTACGACAAGCTGGCAGAGCTTGGCCCACAAGGGCTT
ATCACCACGTTGAAACAACTGGCAGACGGCACGGCGAAACCAGAAGTTCAGGACGAAACT
CTTGTCACTTACGCCGAGAAGTTGAGTAAAGAAGAAGCGCGTATTGACTGGTCACTTTCG
GCAGCACAGCTTGAACGCTGCATTCGCGCTTTCAATCCATGGCCAATGAGCTGGCTGGAA
ATTGAAGGACAGCCGGTTAAAGTCTGGAAAGCATCGGTCATTGATACGGCAACCAACGCT
GCACCAGGAACGATCCTTGAAGCCAACAAACAAGGCATTCAGGTTGCGACTGGTGATGGC
ATCCTGAACCTGCTCTCGTTACAACCTGCGGGTAAGAAAGCGATGAGCGCGCAAGACCTC
CTGAACTCTCGTCGGGAATGGTTTGTTCCGGGCAACCGTCTGGTCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP23882
UniProtKB Entry NameFMT_ECOLI
GenBank Protein ID41474
GenBank Gene IDX63666
General References
  1. Guillon JM, Mechulam Y, Schmitter JM, Blanquet S, Fayat G: Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli. J Bacteriol. 1992 Jul;174(13):4294-301. [Article]
  2. Meinnel T, Guillon JM, Mechulam Y, Blanquet S: The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control. J Bacteriol. 1993 Feb;175(4):993-1000. [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. Mazel D, Pochet S, Marliere P: Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 1994 Feb 15;13(4):914-23. [Article]
  6. Meek DW, Hayward RS: Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second regulatory binding site for protein S4? Nucleic Acids Res. 1984 Jul 25;12(14):5813-21. [Article]
  7. Mazel D, Coic E, Blanchard S, Saurin W, Marliere P: A survey of polypeptide deformylase function throughout the eubacterial lineage. J Mol Biol. 1997 Mar 14;266(5):939-49. [Article]
  8. 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]
  9. Schmitt E, Blanquet S, Mechulam Y: Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase. EMBO J. 1996 Sep 2;15(17):4749-58. [Article]
  10. Schmitt E, Panvert M, Blanquet S, Mechulam Y: Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet. EMBO J. 1998 Dec 1;17(23):6819-26. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04464N-FormylmethionineexperimentalunknownDetails