ID A0A1F6WXQ8_9BACT Unreviewed; 309 AA.
AC A0A1F6WXQ8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00012261, ECO:0000256|HAMAP-Rule:MF_00182};
DE EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261, ECO:0000256|HAMAP-Rule:MF_00182};
GN Name=fmt {ECO:0000256|HAMAP-Rule:MF_00182};
GN ORFNames=A3A91_03050 {ECO:0000313|EMBL:OGI86662.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_01_FULL_36_16.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801767 {ECO:0000313|EMBL:OGI86662.1, ECO:0000313|Proteomes:UP000177001};
RN [1] {ECO:0000313|EMBL:OGI86662.1, ECO:0000313|Proteomes:UP000177001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:0000256|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:0000256|HAMAP-Rule:MF_00182};
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000256|HAMAP-
CC Rule:MF_00182}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGI86662.1}.
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DR EMBL; MFUR01000013; OGI86662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6WXQ8; -.
DR Proteomes; UP000177001; Unassembled WGS sequence.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR Gene3D; 3.40.50.12230; -; 1.
DR HAMAP; MF_00182; Formyl_trans; 1.
DR InterPro; IPR005794; Fmt.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
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; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00182};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000313|EMBL:OGI86662.1}.
FT DOMAIN 101..203
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT BINDING 133..136
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 309 AA; 34861 MW; AFC03D413E249E42 CRC64;
MNKINFIFWG TPDVASETLE ILKQNGLIPS LIVTSPNAPK GRGLRVEASP VALFAEQNNI
TCLKPKKLEK EEIWNVLRTL GRKGGDGQRK FLAKNFRGEQ NIPDFFLVVA YGKIIPENIL
NIPKLGSINA HYSLLPKYRG ASPVESAILN GDTETGITIQ KMIYKMDAGD IIAQEKIEIG
NDEKAGDLRK RLIKIGGELL VKILPEFIEG KIKTIPQDEK EVTFCKKIKK EEGLINLNDD
GILNYNKFRA YAVWPRTFFL ARRSLGEGGF QTRRIIITKA KLENSKFVIE KVLPEGKKEI
SYTEFQKQN
//
