ID   FMT_MAGMM               Reviewed;         312 AA.
AC   A0L3X7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
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};
GN   OrderedLocusNames=Mmc1_0143;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK42670.1; -; Genomic_DNA.
DR   RefSeq; WP_011711843.1; NC_008576.1.
DR   AlphaFoldDB; A0L3X7; -.
DR   SMR; A0L3X7; -.
DR   STRING; 156889.Mmc1_0143; -.
DR   KEGG; mgm:Mmc1_0143; -.
DR   eggNOG; COG0223; Bacteria.
DR   HOGENOM; CLU_033347_1_2_5; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000002586; 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; 3.10.25.10; 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; 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.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..312
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_1000098416"
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   312 AA;  33499 MW;  65CF1B00BBCB1028 CRC64;
     MTAWRVVFMG TPDFATGTLQ ALLDGPDTVV AVFTQPDKPV GRGMKMQKTP VKQLAEQHGI
     PVYQPNRLRE AEAVTALRAL RPDVVVVVAY GQILSREVLE IPTHGCINVH ASLLPRWRGA
     APIQRAILAG DAQSGVTIMA MEEGLDTGPM YSTVVQSIDN HTTGGQLHDQ LMAAGGGLLV
     ETLARIKHEG LTPQIQPEQG VTYAAKLKKE EGLVDWSQPA IQIQRAVQAF DPWPCAFTLW
     QGKPLKLFAA SVVVGHGTPG EVIEVEKDGF VVACGDGALR VAQVQAAGKK RMSSGEWLRG
     HGVKQGERLG EG
//