Methionyl-tRNA formyltransferase (P23882)

Identification
Name:Methionyl-tRNA formyltransferase
Synonyms:Not Available
Gene Name:fmt
Enzyme Class:
Biological Properties
General Function:Involved in methionyl-tRNA formyltransferase 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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0L-Methionyl-tRNA+1.0Thumb ↔ 1.0Thumb+1.0N-Formylmethionyl-tRNA
1.0L-Methionyl-tRNA + 1.0N10-Formyl-THF ↔ 1.0Tetrahydrofolic acid + 1.0N-Formylmethionyl-tRNA
ReactionCard
SMPDB Reactions:
1.0Tetrahydrofolic acid+1.0N-formylmethionyl-tRNA(fMet)+1.0Thumb ? 1.0L-methionyl-tRNA(Met)+1.010-Formyltetrahydrofolate+1.0Thumb
1.0Tetrahydrofolic acid + 1.0N-formylmethionyl-tRNA(fMet) + 1.0Tetrahydrofolic acid ? 1.0L-methionyl-tRNA(Met) + 1.010-Formyltetrahydrofolate + 1.0N10-Formyl-THF
ReactionCard
Complex Reactions:
1.0Thumb+1.0L-Methionyl-tRNA (Met) → 1.0N-Formylmethionyl-tRNA+1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0L-Methionyl-tRNA (Met) → 1.0N-Formylmethionyl-tRNA + 1.0Hydrogen ion + 1.0Tetrahydrofolic acid
ReactionCard
1.0Thumb+1.0L-methionyl-tRNA(fMet) → 1.0Thumb+1.0N-formylmethionyl-tRNA(fMet)
1.0N10-Formyl-THF + 1.0L-methionyl-tRNA(fMet) → 1.0Tetrahydrofolic acid + 1.0N-formylmethionyl-tRNA(fMet)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB00972N10-Formyl-THFMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
GO Classification:
Function
catalytic activity
glycine hydroxymethyltransferase activity
hydroxymethyl-, formyl- and related transferase activity
methionyl-tRNA formyltransferase activity
methyltransferase activity
transferase activity
transferase activity, transferring one-carbon groups
Process
biosynthetic process
cellular macromolecule biosynthetic process
macromolecule biosynthetic process
metabolic process
translation
Gene Properties
Blattner:b3288
Gene OrientationClockwise
Centisome Percentage:73.98
Left Sequence End3432236
Right Sequence End3433183
Gene Sequence:
>948 bp
ATGAGACAAACTCTTTGCGACGGATATCTGGTCATTTTTGCGTTAGCACAGGCCGTGATT
CTGCTGATGCTAACCCCACTTTTTACGGGTATTTCCCGGCAGATACGCGCGCGTATGCAC
TCCCGCCGCGGGCCGGGGATCTGGCAGGATTATCGCGATATCCACAAACTGTTTAAACGC
CAGGAAGTTGCGCCGACATCTTCAGGTCTGATGTTCCGCCTGATGCCGTGGGTATTAATC
AGCAGCATGCTGGTGCTGGCGATGGCCTTACCACTGTTTATTACCGTTTCCCCTTTTGCG
GGCGGCGGCGATCTGATCACCCTTATCTATCTTCTTGCCCTGTTTCGTTTTTTCTTTGCT
CTTTCCGGGCTGGATACCGGAAGTCCGTTTGCGGGAGTCGGTGCCAGTCGCGAGTTGACG
CTCGGCATTCTGGTCGAACCAATGCTTATTCTCTCACTGCTGGTATTGGCGCTGATAGCA
GGTTCCACGCATATCGAGATGATCAGCAATACGCTGGCGATGGGCTGGAACTCGCCGCTA
ACCACCGTACTGGCGTTACTGGCCTGTGGTTTTGCCTGCTTCATTGAGATGGGAAAAATT
CCCTTTGATGTTGCTGAAGCAGAACAGGAATTACAGGAAGGCCCGCTGACCGAATATTCC
GGTGCCGGGCTGGCGCTAGCGAAATGGGGGCTGGGGCTGAAACAGGTCGTGATGGCATCA
CTGTTTGTGGCCCTGTTTCTGCCCTTTGGGCGCGCGCAAGAACTTTCTCTCGCCTGCCTG
CTGACTTCACTTGTCGTTACGCTGCTCAAGGTTTTGCTGATTTTTGTACTGGCCTCAATC
GCAGAAAACACGCTGGCACGCGGGCGTTTTTTACTCATTCACCATGTGACCTGGCTTGGC
TTCAGCCTTGCTGCGCTTGCATGGGTCTTCTGGTTAACCGGTCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:315
Protein Molecular Weight:34168
Protein Theoretical pI:5
PDB File:2FMT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Methionyl-tRNA formyltransferase
MSESLRIIFAGTPDFAARHLDALLSSGHNVVGVFTQPDRPAGRGKKLMPSPVKVLAEEKG
LPVFQPVSLRPQENQQLVAELQADVMVVVAYGLILPKAVLEMPRLGCINVHGSLLPRWRG
AAPIQRSLWAGDAETGVTIMQMDVGLDTGDMLYKLSCPITAEDTSGTLYDKLAELGPQGL
ITTLKQLADGTAKPEVQDETLVTYAEKLSKEEARIDWSLSAAQLERCIRAFNPWPMSWLE
IEGQPVKVWKASVIDTATNAAPGTILEANKQGIQVATGDGILNLLSLQPAGKKAMSAQDL
LNSRREWFVPGNRLV
References
External Links:
ResourceLink
Uniprot ID:P23882
Uniprot Name:FMT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675421
PDB ID:2FMT
Ecogene ID:EG11268
Ecocyc:EG11268
ColiBase:b3288
Kegg Gene:b3288
EchoBASE ID:EB1247
CCDB:FMT_ECOLI
BacMap:16131167
General Reference:
  • 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
  • Guillon, J. M., Mechulam, Y., Schmitter, J. M., Blanquet, S., Fayat, G. (1992). "Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli." J Bacteriol 174:4294-4301. Pubmed: 1624424
  • 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
  • Mazel, D., Coic, E., Blanchard, S., Saurin, W., Marliere, P. (1997). "A survey of polypeptide deformylase function throughout the eubacterial lineage." J Mol Biol 266:939-949. Pubmed: 9086272
  • Mazel, D., Pochet, S., Marliere, P. (1994). "Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation." EMBO J 13:914-923. Pubmed: 8112305
  • Meek, D. W., Hayward, R. S. (1984). "Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second regulatory binding site for protein S4?" Nucleic Acids Res 12:5813-5821. Pubmed: 6379605
  • Meinnel, T., Guillon, J. M., Mechulam, Y., Blanquet, S. (1993). "The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control." J Bacteriol 175:993-1000. Pubmed: 8432722
  • Schmitt, E., Blanquet, S., Mechulam, Y. (1996). "Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase." EMBO J 15:4749-4758. Pubmed: 8887566
  • Schmitt, E., Panvert, M., Blanquet, S., Mechulam, Y. (1998). "Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet." EMBO J 17:6819-6826. Pubmed: 9843487