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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

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

Functioni

Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.UniRule annotation3 Publications

Catalytic activityi

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).UniRule annotation2 Publications

Enzyme regulationi

Activity is optimum in the presence of Mg2+ and K+.1 Publication

Kineticsi

  1. KM=13.5 µM for 10-formyltetrahydrofolate1 Publication
  2. KM=0.35 µM for L-methionyl-tRNA(fMet)1 Publication

    GO - Molecular functioni

    • methionyl-tRNA formyltransferase activity Source: EcoCyc

    GO - Biological processi

    • charged-tRNA amino acid modification Source: EcoCyc

    Keywordsi

    Molecular functionTransferase
    Biological processProtein biosynthesis

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionyl-tRNA formyltransferaseUniRule annotationCurated (EC:2.1.2.9UniRule annotation2 Publications)
    Alternative name(s):
    Met-tRNA(fMet) formyltransferase1 Publication
    Gene namesi
    Name:fmt1 PublicationUniRule annotation
    Synonyms:yhdD
    Ordered Locus Names:b3288, JW3249
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11268. fmt.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    Pathology & Biotechi

    Chemistry databases

    DrugBankiDB04464. N-Formylmethionine.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00000829592 – 315Methionyl-tRNA formyltransferaseAdd BLAST314

    Proteomic databases

    PaxDbiP23882.
    PRIDEiP23882.

    2D gel databases

    SWISS-2DPAGEiP23882.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-9668N.
    IntActiP23882. 12 interactors.
    STRINGi316385.ECDH10B_3462.

    Structurei

    Secondary structure

    1315
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 11Combined sources6
    Helixi14 – 25Combined sources12
    Beta strandi29 – 34Combined sources6
    Beta strandi42 – 44Combined sources3
    Helixi51 – 58Combined sources8
    Beta strandi69 – 71Combined sources3
    Helixi72 – 80Combined sources9
    Beta strandi84 – 90Combined sources7
    Helixi97 – 101Combined sources5
    Beta strandi107 – 114Combined sources8
    Turni115 – 118Combined sources4
    Beta strandi119 – 121Combined sources3
    Helixi123 – 130Combined sources8
    Beta strandi133 – 141Combined sources9
    Beta strandi144 – 147Combined sources4
    Beta strandi151 – 158Combined sources8
    Helixi165 – 189Combined sources25
    Helixi199 – 201Combined sources3
    Helixi210 – 213Combined sources4
    Helixi221 – 230Combined sources10
    Turni231 – 235Combined sources5
    Beta strandi237 – 241Combined sources5
    Beta strandi244 – 254Combined sources11
    Beta strandi264 – 269Combined sources6
    Beta strandi272 – 276Combined sources5
    Beta strandi278 – 289Combined sources12
    Helixi297 – 303Combined sources7
    Helixi305 – 307Combined sources3

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP23882.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni2 – 189N-terminal domain2 PublicationsAdd BLAST188
    Regioni113 – 116Tetrahydrofolate (THF) bindingUniRule annotation4
    Regioni210 – 315C-terminal domain2 PublicationsAdd BLAST106

    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.2 Publications

    Sequence similaritiesi

    Belongs to the Fmt family.UniRule annotationCurated

    Phylogenomic databases

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

    Family and domain databases

    Gene3Di3.10.25.10. 1 hit.
    3.40.50.170. 1 hit.
    HAMAPiMF_00182. Formyl_trans. 1 hit.
    InterProiView protein in InterPro
    IPR005794. Fmt.
    IPR005793. Formyl_trans_C.
    IPR037022. Formyl_trans_C_sf.
    IPR002376. Formyl_transf_N.
    IPR036477. Formyl_transf_N_sf.
    IPR011034. Formyl_transferase-like_C_sf.
    IPR001555. GART_AS.
    PfamiView protein in Pfam
    PF02911. Formyl_trans_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    SUPFAMiSSF50486. SSF50486. 1 hit.
    SSF53328. SSF53328. 1 hit.
    TIGRFAMsiTIGR00460. fmt. 1 hit.
    PROSITEiView protein in PROSITE
    PS00373. GART. 1 hit.

    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.
    PATRICifig|1411691.4.peg.3444.

    Similar proteinsi

    Entry informationi

    Entry nameiFMT_ECOLI
    AccessioniPrimary (citable) accession number: P23882
    Secondary accession number(s): P77040, Q2M6V2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: November 22, 2017
    This is version 160 of the entry and version 4 of the sequence. See 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