FMT_ECOLI
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 03-AUG-2022, entry version 187.
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; Proteobacteria; 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=(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =
CC (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-
CC tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-
CC COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:78530, ChEBI:CHEBI:78844; 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; 45.
DR BioGRID; 852091; 1.
DR DIP; DIP-9668N; -.
DR IntAct; P23882; 12.
DR STRING; 511145.b3288; -.
DR DrugBank; DB04464; N-Formylmethionine.
DR SWISS-2DPAGE; P23882; -.
DR jPOST; P23882; -.
DR PaxDb; P23882; -.
DR PRIDE; P23882; -.
DR EnsemblBacteria; AAC76313; AAC76313; b3288.
DR EnsemblBacteria; BAE78004; BAE78004; BAE78004.
DR GeneID; 947779; -.
DR KEGG; ecj:JW3249; -.
DR KEGG; eco:b3288; -.
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 PhylomeDB; P23882; -.
DR BioCyc; EcoCyc:EG11268-MON; -.
DR BioCyc; MetaCyc:EG11268-MON; -.
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 Gene3D; 3.10.25.10; -; 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 Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF50486; SSF50486; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR TIGRFAMs; TIGR00460; fmt; 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
