Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).

GO - Molecular functioni

  • methionyl-tRNA formyltransferase activity Source: EcoCyc

GO - Biological processi

  • charged-tRNA amino acid modification Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11268-MONOMER.
ECOL316407:JW3249-MONOMER.
MetaCyc:EG11268-MONOMER.
BRENDAi2.1.2.9. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferase (EC:2.1.2.9)
Gene namesi
Name:fmt
Synonyms:yhdD
Ordered Locus Names:b3288, JW3249
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11268. fmt.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 315314Methionyl-tRNA formyltransferasePRO_0000082959Add
BLAST

Proteomic databases

EPDiP23882.
PaxDbiP23882.
PRIDEiP23882.

2D gel databases

SWISS-2DPAGEP23882.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

DIPiDIP-9668N.
IntActiP23882. 12 interactions.
STRINGi511145.b3288.

Structurei

Secondary structure

1
315
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Helixi14 – 2512Combined sources
Beta strandi29 – 346Combined sources
Beta strandi42 – 443Combined sources
Helixi51 – 588Combined sources
Beta strandi69 – 713Combined sources
Helixi72 – 809Combined sources
Beta strandi84 – 907Combined sources
Helixi97 – 1015Combined sources
Beta strandi107 – 1148Combined sources
Turni115 – 1184Combined sources
Beta strandi119 – 1213Combined sources
Helixi123 – 1308Combined sources
Beta strandi133 – 1419Combined sources
Beta strandi144 – 1474Combined sources
Beta strandi151 – 1588Combined sources
Helixi165 – 18925Combined sources
Helixi199 – 2013Combined sources
Helixi210 – 2134Combined sources
Helixi221 – 23010Combined sources
Turni231 – 2355Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi244 – 25411Combined sources
Beta strandi264 – 2696Combined sources
Beta strandi272 – 2765Combined sources
Beta strandi278 – 28912Combined sources
Helixi297 – 3037Combined sources
Helixi305 – 3073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FMTX-ray2.00A/B2-315[»]
2FMTX-ray2.80A/B2-315[»]
ProteinModelPortaliP23882.
SMRiP23882. Positions 2-315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23882.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 189188N-terminal domainAdd
BLAST
Regioni113 – 1164Tetrahydrofolate (THF) binding
Regioni210 – 315106C-terminal domainAdd
BLAST

Domaini

Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction.

Sequence similaritiesi

Belongs to the Fmt family.Curated

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
InParanoidiP23882.
KOiK00604.
OMAiGCINSHA.
OrthoDBiEOG6B09WV.
PhylomeDBiP23882.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23882-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESLRIIFA GTPDFAARHL DALLSSGHNV VGVFTQPDRP AGRGKKLMPS
60 70 80 90 100
PVKVLAEEKG LPVFQPVSLR PQENQQLVAE LQADVMVVVA YGLILPKAVL
110 120 130 140 150
EMPRLGCINV HGSLLPRWRG AAPIQRSLWA GDAETGVTIM QMDVGLDTGD
160 170 180 190 200
MLYKLSCPIT AEDTSGTLYD KLAELGPQGL ITTLKQLADG TAKPEVQDET
210 220 230 240 250
LVTYAEKLSK EEARIDWSLS AAQLERCIRA FNPWPMSWLE IEGQPVKVWK
260 270 280 290 300
ASVIDTATNA APGTILEANK QGIQVATGDG ILNLLSLQPA GKKAMSAQDL
310
LNSRREWFVP GNRLV
Length:315
Mass (Da):34,168
Last modified:January 23, 2007 - v4
Checksum:i1AE14C808F04A126
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63666 Genomic DNA. Translation: CAA45207.1.
X77091 Genomic DNA. Translation: CAA54368.1.
U18997 Genomic DNA. Translation: AAA58085.1.
U00096 Genomic DNA. Translation: AAC76313.1.
AP009048 Genomic DNA. Translation: BAE78004.1.
X00767 Genomic DNA. Translation: CAA25339.1. Sequence problems.
Y10307 Genomic DNA. Translation: CAA71358.1.
PIRiS23108.
RefSeqiNP_417746.1. NC_000913.3.
WP_000004473.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76313; AAC76313; b3288.
BAE78004; BAE78004; BAE78004.
GeneIDi947779.
KEGGiecj:JW3249.
eco:b3288.
PATRICi32122008. VBIEscCol129921_3381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63666 Genomic DNA. Translation: CAA45207.1.
X77091 Genomic DNA. Translation: CAA54368.1.
U18997 Genomic DNA. Translation: AAA58085.1.
U00096 Genomic DNA. Translation: AAC76313.1.
AP009048 Genomic DNA. Translation: BAE78004.1.
X00767 Genomic DNA. Translation: CAA25339.1. Sequence problems.
Y10307 Genomic DNA. Translation: CAA71358.1.
PIRiS23108.
RefSeqiNP_417746.1. NC_000913.3.
WP_000004473.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FMTX-ray2.00A/B2-315[»]
2FMTX-ray2.80A/B2-315[»]
ProteinModelPortaliP23882.
SMRiP23882. Positions 2-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9668N.
IntActiP23882. 12 interactions.
STRINGi511145.b3288.

2D gel databases

SWISS-2DPAGEP23882.

Proteomic databases

EPDiP23882.
PaxDbiP23882.
PRIDEiP23882.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76313; AAC76313; b3288.
BAE78004; BAE78004; BAE78004.
GeneIDi947779.
KEGGiecj:JW3249.
eco:b3288.
PATRICi32122008. VBIEscCol129921_3381.

Organism-specific databases

EchoBASEiEB1247.
EcoGeneiEG11268. fmt.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
InParanoidiP23882.
KOiK00604.
OMAiGCINSHA.
OrthoDBiEOG6B09WV.
PhylomeDBiP23882.

Enzyme and pathway databases

BioCyciEcoCyc:EG11268-MONOMER.
ECOL316407:JW3249-MONOMER.
MetaCyc:EG11268-MONOMER.
BRENDAi2.1.2.9. 2026.

Miscellaneous databases

EvolutionaryTraceiP23882.
PROiP23882.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli."
    Guillon J.-M., Mechulam Y., Schmitter J.-M., Blanquet S., Fayat G.
    J. Bacteriol. 174:4294-4301(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12 / K37.
  2. "The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control."
    Meinnel T., Guillon J.-M., Mechulam Y., Blanquet S.
    J. Bacteriol. 175:993-1000(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / K37.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation."
    Mazel D., Pochet S., Marliere P.
    EMBO J. 13:914-923(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
  6. "Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second regulatory binding site for protein S4?"
    Meek D.W., Hayward R.S.
    Nucleic Acids Res. 12:5813-5821(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-162.
  7. "A survey of polypeptide deformylase function throughout the eubacterial lineage."
    Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.
    J. Mol. Biol. 266:939-949(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-315.
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase."
    Schmitt E., Blanquet S., Mechulam Y.
    EMBO J. 15:4749-4758(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  10. "Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet."
    Schmitt E., Panvert M., Blanquet S., Mechulam Y.
    EMBO J. 17:6819-6826(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiFMT_ECOLI
AccessioniPrimary (citable) accession number: P23882
Secondary accession number(s): P77040, Q2M6V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.