ID   FMT_XANC5               Reviewed;         307 AA.
AC   Q3BNK7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=XCV3925;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ25656.1; -; Genomic_DNA.
DR   RefSeq; WP_011348782.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BNK7; -.
DR   SMR; Q3BNK7; -.
DR   STRING; 456327.BJD11_03015; -.
DR   EnsemblBacteria; CAJ25656; CAJ25656; XCV3925.
DR   KEGG; xcv:XCV3925; -.
DR   eggNOG; COG0223; Bacteria.
DR   HOGENOM; CLU_033347_1_2_6; -.
DR   OMA; CCPVVAY; -.
DR   Proteomes; UP000007069; 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; -; 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; 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..307
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_1000020203"
FT   BINDING         108..111
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   307 AA;  32793 MW;  A3F0DEF10E691485 CRC64;
     MRIIFAGTPD FAVPSLRAAA QRHEVVAVYT QPDRPAGRGR GLTPSPVKLE AVARGIPVFQ
     PQTLRSPEAL ATVRKLDADL MVVVAYGLIL PKAVLAAPTH GCWNVHASLL PRWRGAAPIQ
     RAIEAGDTET GVCLMQMEAG LDTGPVLLSQ RIEIGEQETG GQLHDRLAAL GAQVLSDGLG
     LLRAGIRPVA QPQPDDGVTY AHKLDKAQAR LDWAQPAQEL ARRVRAFNPW PVAEAILAGE
     RVRLHGAVAL ELAHQHPPGT LLAASKQGID IACGEGALRV RVLQREGGKA ITAADYLNAR
     RDLPALR