ID   FMT_VIBAL               Reviewed;         247 AA.
AC   O87726;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000250|UniProtKB:P23882};
DE            EC=2.1.2.9 {ECO:0000250|UniProtKB:P23882};
DE   Flags: Fragment;
GN   Name=fmt;
OS   Vibrio alginolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=138-2;
RX   PubMed=9720051; DOI=10.1099/00221287-144-8-2281;
RA   Nakamura T., Yamamuro N., Stumpe S., Unemoto T., Bakker E.P.;
RT   "Cloning of the trkAH gene cluster and characterization of the Trk K+-
RT   uptake system of Vibrio alginolyticus.";
RL   Microbiology 144:2281-2289(1998).
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; D86411; BAA31225.1; -; Genomic_DNA.
DR   AlphaFoldDB; O87726; -.
DR   SMR; O87726; -.
DR   STRING; 663.BAU10_14915; -.
DR   eggNOG; COG0223; Bacteria.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC.
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; IPR001555; GART_AS.
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.
DR   PROSITE; PS00373; GART; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Transferase.
FT   CHAIN           <1..247
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_0000083079"
FT   NON_TER         1
SQ   SEQUENCE   247 AA;  26929 MW;  2FB9D3A022A4DEE6 CRC64;
     SFKSDEAKQE LADLNADLMV FVAYGMLLPQ AVLDTPKLGC INVHGSILPR WRCAAPIQRS
     IWAGDAETGV TIMQMDIGLD TGDMLKIATL PIETTDTSAS MYEKLAELGP EALIDCLADI
     AAGKAVPVKQ DDELANYAKK LSKEEARINW NDDAAHIERC VRAFNPWPMS HFEAAENSIK
     VWKAVWQSKP VTTSGTIVQA DKTGIYVVTG NGVLVLEQLQ VPGKKAMSVQ DILNSRAAWF
     EVGTLLV