ID   FMT_CHLSY               Reviewed;         310 AA.
AC   B9LFJ4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Chy400_0038;
OS   Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=480224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29364 / DSM 637 / Y-400-fl;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroflexus sp. Y-400-fl.";
RL   Submitted (JAN-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; CP001364; ACM51482.1; -; Genomic_DNA.
DR   RefSeq; WP_012255944.1; NC_012032.1.
DR   AlphaFoldDB; B9LFJ4; -.
DR   SMR; B9LFJ4; -.
DR   KEGG; chl:Chy400_0038; -.
DR   HOGENOM; CLU_033347_1_1_0; -.
DR   OMA; CCPVVAY; -.
DR   OrthoDB; 2009156at2; -.
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; -; 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   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..310
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_1000190016"
FT   BINDING         109..112
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   310 AA;  33137 MW;  C238A6878775B27A CRC64;
     MRILFLGSPS FAVHALEALV AAGHEIVGVV TQPDRPAGRD RRLTPPPVKI AAMAHNLPVL
     QPETLRDPTV VETLSALQPE VGVVAAYGEI LRRAVLSIPP LGYLNIHPSL LPLYRGPTPV
     AGAILAGETV TGVTIMLLDP SMDSGPILAQ AVVDLPPTAR AGQLTDELFR IGADLLVQVL
     PRYARGEIEP RPQDHSRATV TKMLKKEDGR IDWSLPAIVI ERMTRAYDPW PGAYTFWRGQ
     PLRIIKAAVA SADGTNVPGT VIGRSGSGHP LVQTGSDALE LIEVQPASRR PMSGSAWLAG
     VHADNIRLGE