FMT_BACFR
ID FMT_BACFR Reviewed; 324 AA.
AC Q64PD6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=BF3903;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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=(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; AP006841; BAD50645.1; -; Genomic_DNA.
DR RefSeq; WP_008770001.1; NZ_UYXF01000018.1.
DR RefSeq; YP_101179.1; NC_006347.1.
DR AlphaFoldDB; Q64PD6; -.
DR SMR; Q64PD6; -.
DR STRING; 295405.BF3903; -.
DR EnsemblBacteria; BAD50645; BAD50645; BF3903.
DR GeneID; 66331491; -.
DR KEGG; bfr:BF3903; -.
DR PATRIC; fig|295405.11.peg.3747; -.
DR HOGENOM; CLU_033347_1_1_10; -.
DR OMA; CCPVVAY; -.
DR Proteomes; UP000002197; 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 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; 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..324
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000082913"
FT BINDING 113..116
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ SEQUENCE 324 AA; 36389 MW; 324EA580827CBF1E CRC64;
MKKEDLRIVY MGTPDFAVEA LQCLVEGGYN VVGVITMPDK PAGRGHKIQY SPVKQYALDH
QLPLLQPEKL KDEEFIQALR EWKADLQIVV AFRMLPEVVW NMPRLGTFNL HASLLPQYRG
AAPINWAVIN GDTETGITTF FLKHEIDTGE VIQQVRIPIA DTDNVEIVHD KLMHLGGRLV
IETVDAILEG KVKSIPQEEM AVAGELRPAP KIFKETCRID WNQPVKRVYD FIRGLSPYPA
AWSELVNPEG EAVVVKIFES EKLPKVHTLA PGSIVTDGKN FLRVAVPDGF VNVLSLQLPG
KKRLKTDELL RGFHLTEAFK MKAV
