ID   FMT_ECOLI               Reviewed;         315 AA.
AC   P23882; P77040; Q2M6V2;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-NOV-2024, entry version 196.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000255|HAMAP-Rule:MF_00182, ECO:0000305};
DE            EC=2.1.2.9 {ECO:0000255|HAMAP-Rule:MF_00182, ECO:0000269|PubMed:6989606, ECO:0000269|PubMed:9843487};
DE   AltName: Full=Met-tRNA(fMet) formyltransferase {ECO:0000303|PubMed:1624424};
GN   Name=fmt {ECO:0000255|HAMAP-Rule:MF_00182, ECO:0000303|PubMed:1624424};
GN   Synonyms=yhdD; OrderedLocusNames=b3288, JW3249;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=K12 / K37;
RX   PubMed=1624424; DOI=10.1128/jb.174.13.4294-4301.1992;
RA   Guillon J.-M., Mechulam Y., Schmitter J.-M., Blanquet S., Fayat G.;
RT   "Disruption of the gene for Met-tRNA(fMet) formyltransferase severely
RT   impairs growth of Escherichia coli.";
RL   J. Bacteriol. 174:4294-4301(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / K37;
RX   PubMed=8432722; DOI=10.1128/jb.175.4.993-1000.1993;
RA   Meinnel T., Guillon J.-M., Mechulam Y., Blanquet S.;
RT   "The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet)
RT   formyltransferase, escapes metabolic control.";
RL   J. Bacteriol. 175:993-1000(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
RX   PubMed=8112305; DOI=10.1002/j.1460-2075.1994.tb06335.x;
RA   Mazel D., Pochet S., Marliere P.;
RT   "Genetic characterization of polypeptide deformylase, a distinctive enzyme
RT   of eubacterial translation.";
RL   EMBO J. 13:914-923(1994).
RN   [6]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-162.
RX   PubMed=6379605; DOI=10.1093/nar/12.14.5813;
RA   Meek D.W., Hayward R.S.;
RT   "Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second
RT   regulatory binding site for protein S4?";
RL   Nucleic Acids Res. 12:5813-5821(1984).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-315.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9086272; DOI=10.1006/jmbi.1996.0835;
RA   Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.;
RT   "A survey of polypeptide deformylase function throughout the eubacterial
RT   lineage.";
RL   J. Mol. Biol. 266:939-949(1997).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RX   PubMed=6989606; DOI=10.1111/j.1432-1033.1980.tb04524.x;
RA   Kahn D., Fromant M., Fayat G., Dessen P., Blanquet S.;
RT   "Methionyl-transfer-RNA transformylase from Escherichia coli. Purification
RT   and characterisation.";
RL   Eur. J. Biochem. 105:489-497(1980).
RN   [9]
RP   FUNCTION.
RX   PubMed=8331078; DOI=10.1128/jb.175.14.4507-4514.1993;
RA   Guillon J.M., Mechulam Y., Blanquet S., Fayat G.;
RT   "Importance of formylability and anticodon stem sequence to give a
RT   tRNA(Met) an initiator identity in Escherichia coli.";
RL   J. Bacteriol. 175:4507-4514(1993).
RN   [10]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [11] {ECO:0007744|PDB:1FMT}
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DOMAIN.
RX   PubMed=8887566; DOI=10.1002/j.1460-2075.1996.tb00852.x;
RA   Schmitt E., Blanquet S., Mechulam Y.;
RT   "Structure of crystalline Escherichia coli methionyl-tRNA(f)Met
RT   formyltransferase: comparison with glycinamide ribonucleotide
RT   formyltransferase.";
RL   EMBO J. 15:4749-4758(1996).
RN   [12] {ECO:0007744|PDB:2FMT}
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP   DOMAIN.
RX   PubMed=9843487; DOI=10.1093/emboj/17.23.6819;
RA   Schmitt E., Panvert M., Blanquet S., Mechulam Y.;
RT   "Crystal structure of methionyl-tRNAfMet transformylase complexed with the
RT   initiator formyl-methionyl-tRNAfMet.";
RL   EMBO J. 17:6819-6826(1998).
CC   -!- FUNCTION: Attaches a formyl group to the free amino group of methionyl-
CC       tRNA(fMet). The formyl group appears to play a dual role in the
CC       initiator identity of N-formylmethionyl-tRNA by promoting its
CC       recognition by IF2 and preventing the misappropriation of this tRNA by
CC       the elongation apparatus. {ECO:0000255|HAMAP-Rule:MF_00182,
CC       ECO:0000269|PubMed:6989606, ECO:0000269|PubMed:8331078,
CC       ECO:0000269|PubMed:9843487}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionyl-tRNA(fMet) + (6R)-10-formyltetrahydrofolate = N-
CC         formyl-L-methionyl-tRNA(fMet) + (6S)-5,6,7,8-tetrahydrofolate + H(+);
CC         Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-COMP:9953,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; EC=2.1.2.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00182,
CC         ECO:0000269|PubMed:6989606, ECO:0000269|PubMed:9843487};
CC   -!- ACTIVITY REGULATION: Activity is optimum in the presence of Mg(2+) and
CC       K(+). {ECO:0000269|PubMed:6989606}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.5 uM for 10-formyltetrahydrofolate
CC         {ECO:0000269|PubMed:6989606};
CC         KM=0.35 uM for L-methionyl-tRNA(fMet) {ECO:0000269|PubMed:6989606};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:6989606}.
CC   -!- DOMAIN: Composed of an N- and a C-terminal domain. The N-terminal
CC       domain carries the tetrahydrofolate (THF)-binding site and the C-
CC       terminal domain is presumably involved in positioning the Met-tRNA
CC       substrate for the formylation reaction. {ECO:0000269|PubMed:8887566,
CC       ECO:0000269|PubMed:9843487}.
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC       Rule:MF_00182, ECO:0000305}.
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DR   EMBL; X63666; CAA45207.1; -; Genomic_DNA.
DR   EMBL; X77091; CAA54368.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58085.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76313.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78004.1; -; Genomic_DNA.
DR   EMBL; X00767; CAA25339.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; Y10307; CAA71358.1; -; Genomic_DNA.
DR   PIR; S23108; S23108.
DR   RefSeq; NP_417746.1; NC_000913.3.
DR   RefSeq; WP_000004473.1; NZ_SSZK01000040.1.
DR   PDB; 1FMT; X-ray; 2.00 A; A/B=2-315.
DR   PDB; 2FMT; X-ray; 2.80 A; A/B=2-315.
DR   PDBsum; 1FMT; -.
DR   PDBsum; 2FMT; -.
DR   AlphaFoldDB; P23882; -.
DR   SMR; P23882; -.
DR   BioGRID; 4263429; 57.
DR   BioGRID; 852091; 1.
DR   DIP; DIP-9668N; -.
DR   IntAct; P23882; 12.
DR   STRING; 511145.b3288; -.
DR   DrugBank; DB04464; N-Formylmethionine.
DR   jPOST; P23882; -.
DR   PaxDb; 511145-b3288; -.
DR   EnsemblBacteria; AAC76313; AAC76313; b3288.
DR   GeneID; 947779; -.
DR   KEGG; ecj:JW3249; -.
DR   KEGG; eco:b3288; -.
DR   KEGG; ecoc:C3026_17875; -.
DR   PATRIC; fig|1411691.4.peg.3444; -.
DR   EchoBASE; EB1247; -.
DR   eggNOG; COG0223; Bacteria.
DR   HOGENOM; CLU_033347_1_2_6; -.
DR   InParanoid; P23882; -.
DR   OMA; CCPVVAY; -.
DR   OrthoDB; 9802815at2; -.
DR   PhylomeDB; P23882; -.
DR   BioCyc; EcoCyc:EG11268-MONOMER; -.
DR   BioCyc; MetaCyc:EG11268-MONOMER; -.
DR   BRENDA; 2.1.2.9; 2026.
DR   EvolutionaryTrace; P23882; -.
DR   PRO; PR:P23882; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0019988; P:charged-tRNA amino acid modification; IDA:EcoCyc.
DR   GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; IMP:EcoCyc.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR   CDD; cd08704; Met_tRNA_FMT_C; 1.
DR   FunFam; 3.10.25.10:FF:000001; Methionyl-tRNA formyltransferase; 1.
DR   FunFam; 3.40.50.12230:FF:000001; Methionyl-tRNA formyltransferase; 1.
DR   FunFam; 3.40.50.170:FF:000003; Methionyl-tRNA formyltransferase; 1.
DR   Gene3D; 3.10.25.10; Formyl transferase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR   HAMAP; MF_00182; Formyl_trans; 1.
DR   InterPro; IPR005794; Fmt.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR037022; Formyl_trans_C_sf.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR001555; GART_AS.
DR   InterPro; IPR044135; Met-tRNA-FMT_C.
DR   InterPro; IPR041711; Met-tRNA-FMT_N.
DR   NCBIfam; TIGR00460; fmt; 1.
DR   PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   PROSITE; PS00373; GART; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Protein biosynthesis;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..315
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_0000082959"
FT   REGION          2..189
FT                   /note="N-terminal domain"
FT                   /evidence="ECO:0000305|PubMed:8887566,
FT                   ECO:0000305|PubMed:9843487"
FT   REGION          210..315
FT                   /note="C-terminal domain"
FT                   /evidence="ECO:0000305|PubMed:8887566,
FT                   ECO:0000305|PubMed:9843487"
FT   BINDING         113..116
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   HELIX           14..25
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:2FMT"
FT   HELIX           51..58
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:2FMT"
FT   HELIX           72..80
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   HELIX           97..101
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   TURN            115..118
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   HELIX           123..130
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          133..141
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          151..158
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   HELIX           165..189
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   HELIX           210..213
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   HELIX           221..230
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   TURN            231..235
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          244..254
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          264..269
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          272..276
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   STRAND          278..289
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   HELIX           297..303
FT                   /evidence="ECO:0007829|PDB:1FMT"
FT   HELIX           305..307
FT                   /evidence="ECO:0007829|PDB:1FMT"
SQ   SEQUENCE   315 AA;  34168 MW;  1AE14C808F04A126 CRC64;
     MSESLRIIFA GTPDFAARHL DALLSSGHNV VGVFTQPDRP AGRGKKLMPS PVKVLAEEKG
     LPVFQPVSLR PQENQQLVAE LQADVMVVVA YGLILPKAVL EMPRLGCINV HGSLLPRWRG
     AAPIQRSLWA GDAETGVTIM QMDVGLDTGD MLYKLSCPIT AEDTSGTLYD KLAELGPQGL
     ITTLKQLADG TAKPEVQDET LVTYAEKLSK EEARIDWSLS AAQLERCIRA FNPWPMSWLE
     IEGQPVKVWK ASVIDTATNA APGTILEANK QGIQVATGDG ILNLLSLQPA GKKAMSAQDL
     LNSRREWFVP GNRLV
//