FMT_THET8
ID FMT_THET8 Reviewed; 305 AA.
AC Q5SLH3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=TTHA0320;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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; AP008226; BAD70143.1; -; Genomic_DNA.
DR RefSeq; WP_011227858.1; NC_006461.1.
DR RefSeq; YP_143586.1; NC_006461.1.
DR AlphaFoldDB; Q5SLH3; -.
DR SMR; Q5SLH3; -.
DR STRING; 300852.55771702; -.
DR EnsemblBacteria; BAD70143; BAD70143; BAD70143.
DR GeneID; 3169685; -.
DR KEGG; ttj:TTHA0320; -.
DR PATRIC; fig|300852.9.peg.320; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_2_0_0; -.
DR OMA; CCPVVAY; -.
DR PhylomeDB; Q5SLH3; -.
DR Proteomes; UP000000532; 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; Reference proteome; Transferase.
FT CHAIN 1..305
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000083073"
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 305 AA; 33295 MW; EDF66B031BBE6BD5 CRC64;
MRVAFFGTPL WAVPVLDALR KRHQVVLVVS QPDKPQGRGL RPAPSPVARY AEAEGLPLLR
PARLREEAFL EALRQAAPEV AVVAAYGKLI PKEALDIPPH GFLNLHPSLL PKYRGAAPVQ
RALLAGERET GVSIMRLDEG LDTGPLYAVW RTPILPDEDA VALGNRLRDK GVELLLEVLE
RLPELTPRPQ EGEASYAPPL SKEEGRLDFG ESAEALYRRH RAVQPWPGSY FFHRGQRVKA
LRLRPEPGEG EPGVVARVGP EGVVVGTASG LLLLLEVQPE GRRAMPAADW ARGYGVAPGT
RLGQV
