ID FMT_CLOAB Reviewed; 310 AA.
AC O05101;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 27-MAR-2024, entry version 136.
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=CA_C1723;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-173.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=9504995; DOI=10.1007/s002849900304;
RA Belouski E., Gui L., Rudolph F.B., Bennett G.N.;
RT "Complementation of an Escherichia coli polypeptide deformylase mutant with
RT a gene from Clostridium acetobutylicum ATCC 824.";
RL Curr. Microbiol. 36:248-249(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:0000255|HAMAP-Rule:MF_00182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-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:78530,
CC ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; 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, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB50348.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001437; AAK79689.1; -; Genomic_DNA.
DR EMBL; U52368; AAB50348.1; ALT_INIT; Genomic_DNA.
DR PIR; F97112; F97112.
DR RefSeq; NP_348349.1; NC_003030.1.
DR RefSeq; WP_010965030.1; NC_003030.1.
DR AlphaFoldDB; O05101; -.
DR SMR; O05101; -.
DR STRING; 272562.CA_C1723; -.
DR GeneID; 44998218; -.
DR KEGG; cac:CA_C1723; -.
DR PATRIC; fig|272562.8.peg.1925; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_1_9; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000000814; 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; 3.40.50.12230; -; 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 NCBIfam; TIGR00460; fmt; 1.
DR PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000082949"
FT BINDING 110..113
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ SEQUENCE 310 AA; 34391 MW; B94ACAC269659F65 CRC64;
MLKIVFMGTP EFSVPSLEKL IENYDVRAVL TQPDKPKGRG KKLAMSEVKE VAVKNNIPVF
QPVKLKNDIE VINKLKEIAP DFIVVVAFGQ ILSKEVLDIP KYACINLHAS LLPNYRGAAP
INWAIINGET KTGNTTMIMA EGLDTGDMLL KDEVDIKRDM TAGELHDILM NRGADLLVKT
IDEFSKGNIK PEKQGEPETD YAAMLSKDTG KINWNDKSER IYNLIRGLNP WPLAYSSYND
KVMKIHEAKI LDAAPEGEPG LITNVDNNGI EVNSSDGKIL ITKIQFPGKK SMNVGEYIRG
NNIDKGVILK
//
