FMT_BURP1
ID FMT_BURP1 Reviewed; 327 AA.
AC Q3JXE1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=BURPS1710b_0347;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000124; ABA47683.1; -; Genomic_DNA.
DR RefSeq; WP_004525853.1; NC_007434.1.
DR AlphaFoldDB; Q3JXE1; -.
DR SMR; Q3JXE1; -.
DR EnsemblBacteria; ABA47683; ABA47683; BURPS1710b_0347.
DR KEGG; bpm:BURPS1710b_0347; -.
DR HOGENOM; CLU_033347_1_2_4; -.
DR OMA; CCPVVAY; -.
DR OrthoDB; 2009156at2; -.
DR Proteomes; UP000002700; Chromosome I.
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..327
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_1000020034"
FT BINDING 121..124
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ SEQUENCE 327 AA; 33934 MW; 2F0B67692E173DCF CRC64;
MTHSLRVIFA GTPEFAAAAL AAIHEAGFPV PLVLTQPDRP AGRGMKLQAS AVKRYAFERG
MAVAQPPSLR RAGKYPAEAV AALDLLHATP HDVMVVAAYG LLLPQEVLEL PRHGCINIHA
SLLPRWRGAA PIHRAIEAGD AETGVTLMQM DAGLDTGAML HEARVAIAPD DTTATLHDKL
AAAGARLVVD ALVELERTGA LAATPQPADG VTYAEKIGKH EAALDWRKPA AALARQVRAF
DPFPGGAGTL DGATLKLWAA DAVPGRDDAA PGTIVDIGPD GVVIACGEGA LRVTQLQKPG
GKRLPAREFL AGAPLAVGQR FAPADAA
