ID FMT_MYCMS Reviewed; 317 AA.
AC Q6MTF8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 106.
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=MSC_0450;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
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=(6R)-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:78530,
CC ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; 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; BX293980; CAE77078.1; -; Genomic_DNA.
DR RefSeq; NP_975436.1; NC_005364.2.
DR AlphaFoldDB; Q6MTF8; -.
DR SMR; Q6MTF8; -.
DR STRING; 272632.MSC_0450; -.
DR KEGG; mmy:MSC_0450; -.
DR PATRIC; fig|272632.4.peg.490; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_1_14; -.
DR Proteomes; UP000001016; 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 Gene3D; 3.40.50.12230; -; 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; 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 3: Inferred from homology;
KW Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000082994"
FT BINDING 112..115
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ SEQUENCE 317 AA; 35832 MW; 9A4DD908C9AAA65F CRC64;
MQNKIKVVFC GTPKIGADVL KALIEMNQVE IVLVISQPDK PIGRKKQIVH TPVKKLALEN
NLKVVQPNKI GEIYDDLAKL EFDFLITCAF GQFIPTKILK LAKIDSINFH GSLLPKLRGG
APIQYAIKNG DKKTGITIMQ MVKQMDAGDY YVQESIDILD SDDSGSLFEK MGHLAYSMCK
KYLVDIYNHK FELIKQNEDE VTFCKNISSE EEKINWNNTS LDIFNLIRSL SPSPISYTTI
NNQRYKIKSS KVIDLDNQNK NAIPGTILGI NKQGIVVKTL DKALLILEIQ KEGKKMILAS
NYYLNKLSDL KINDKFD
//
