FMT_SALTY
ID FMT_SALTY Reviewed; 315 AA.
AC Q8ZLM6;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 118.
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=STM3407;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- DOMAIN: Composed of an N- and a C-terminal domain. The N-terminal
CC domain carries the tetrahydrofolate (THF)-binding site and the C-
CC terminal domain is presumably involved in positioning the Met-tRNA
CC substrate for the formylation reaction.
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC Rule:MF_00182, ECO:0000305}.
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DR EMBL; AE006468; AAL22270.1; -; Genomic_DNA.
DR RefSeq; NP_462311.1; NC_003197.2.
DR RefSeq; WP_001285165.1; NC_003197.2.
DR AlphaFoldDB; Q8ZLM6; -.
DR SMR; Q8ZLM6; -.
DR STRING; 99287.STM3407; -.
DR PaxDb; Q8ZLM6; -.
DR EnsemblBacteria; AAL22270; AAL22270; STM3407.
DR GeneID; 1254930; -.
DR KEGG; stm:STM3407; -.
DR PATRIC; fig|99287.12.peg.3605; -.
DR HOGENOM; CLU_033347_1_2_6; -.
DR OMA; CCPVVAY; -.
DR PhylomeDB; Q8ZLM6; -.
DR BioCyc; SENT99287:STM3407-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IBA:GO_Central.
DR GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; IBA:GO_Central.
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; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..315
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000083041"
FT REGION 2..189
FT /note="N-terminal domain"
FT REGION 210..315
FT /note="C-terminal domain"
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 315 AA; 34029 MW; 10A4E596AFEDB117 CRC64;
MSDSLRIIFA GTPDFAARHL DALLTSGHNV VGVFTQPDRP AGRGKKLMPS PVKVLAEEKG
LPVFQPVSLR PQENQHLVAD LHADVMVVVA YGLILPKAVL DMPRLGCINV HGSLLPRWRG
AAPIQRSLWA GDAETGVTIM QMDVGLDTGD MLYKLACPIT AEDTSGSLYN KLAELGPQGL
ITTLKQLADG TATPEAQNEA LVTHAEKLSK EEARIDWSLS AAQLERCIRA FNPWPMSWLE
IDGQPVKVWQ ASVIEDATQS LPGTILAATK QGIQVATGKG ILNLLSLQPA GKKAMSAQDL
LNSRREWFIP GNRLA
