ID   FMT_MYCGE               Reviewed;         311 AA.
AC   P47605;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000250|UniProtKB:P23882};
DE            EC=2.1.2.9 {ECO:0000250|UniProtKB:P23882};
GN   Name=fmt; OrderedLocusNames=MG365;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
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:0000250|UniProtKB:P23882}.
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:0000250|UniProtKB:P23882};
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}.
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DR   EMBL; L43967; AAC71592.1; -; Genomic_DNA.
DR   PIR; D64240; D64240.
DR   RefSeq; WP_010869450.1; NC_000908.2.
DR   AlphaFoldDB; P47605; -.
DR   SMR; P47605; -.
DR   STRING; 243273.MG_365; -.
DR   EnsemblBacteria; AAC71592; AAC71592; MG_365.
DR   KEGG; mge:MG_365; -.
DR   eggNOG; COG0223; Bacteria.
DR   HOGENOM; CLU_033347_1_1_14; -.
DR   OMA; CCPVVAY; -.
DR   OrthoDB; 2009156at2; -.
DR   BioCyc; MGEN243273:G1GJ2-459-MON; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IBA:GO_Central.
DR   GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; IBA:GO_Central.
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   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; 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; Reference proteome; Transferase.
FT   CHAIN           1..311
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_0000082993"
FT   BINDING         109..112
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:P23882"
SQ   SEQUENCE   311 AA;  35536 MW;  38D96D99DCDC1EE0 CRC64;
     MFKIVFFGTS TLSKKCLEQL FYDNDFEICA VVTQPDKINH RNNKIVPSDV KSFCLEKNIT
     FFQPKQSISI KADLEKLKAD IGICVSFGQY LHQDIIDLFP NKVINLHPSK LPLLRGGAPL
     HWTIINGFKK SALSVIQLVK KMDAGPIWKQ QDFLVNNDWN TGDLSIYVEE HSPSFLIECT
     KEILNKKGKW FEQIGEPTFG LNIRKEQEHL DLNQIYKSFL NWVKGLAPKP GGWLSFEGKN
     IKIFKAKYVS KSNYKHQLGE IVNISRKGIN IALKSNEIIS IEKIQIPGKR VMEVSEIING
     KHPFVVGKCF K