ID   FMT_RHOOB               Reviewed;         307 AA.
AC   C1B4K2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000255|HAMAP-Rule:MF_00182};
DE            EC=2.1.2.9 {ECO:0000255|HAMAP-Rule:MF_00182};
GN   Name=fmt {ECO:0000255|HAMAP-Rule:MF_00182}; OrderedLocusNames=ROP_69440;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC       Rule:MF_00182}.
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DR   EMBL; AP011115; BAH55191.1; -; Genomic_DNA.
DR   RefSeq; WP_015890617.1; NC_012522.1.
DR   AlphaFoldDB; C1B4K2; -.
DR   SMR; C1B4K2; -.
DR   STRING; 632772.ROP_69440; -.
DR   PRIDE; C1B4K2; -.
DR   EnsemblBacteria; BAH55191; BAH55191; ROP_69440.
DR   KEGG; rop:ROP_69440; -.
DR   PATRIC; fig|632772.20.peg.7235; -.
DR   HOGENOM; CLU_033347_1_0_11; -.
DR   OMA; CCPVVAY; -.
DR   OrthoDB; 2009156at2; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR   CDD; cd08704; Met_tRNA_FMT_C; 1.
DR   HAMAP; MF_00182; Formyl_trans; 1.
DR   InterPro; IPR005794; Fmt.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
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.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Transferase.
FT   CHAIN           1..307
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_1000190037"
FT   BINDING         110..113
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   307 AA;  32347 MW;  AF9232ED62776D12 CRC64;
     MRIVFAGTPE PAVPSLERLI RSPRHDVVAV ITRPDAVAGR GRKVVRSPIG ALADSHGIEV
     LTPERPTEPE FLARLTDLAP DCAPVVAYGA LLPQKVLDIP AHGWVNLHFS LLPAWRGAAP
     VQAAIGAGDD MTGASAFRLE AGMDTGPVYG VVTERIRDTD TAGDLLGRLA DSGAALLESV
     LDGIEDGAIT AVPQPAEGVS HAAKVTVEAA RIRWDRPAAV VDRHVRSVTP GPGAWTTIGD
     VRLKVGPVTP TDERLEPGEI SVTKSGFLIG TSTAAVRLDR VQPQGKKQMA ALDWARGARL
     DAEVRAQ