ID A0A0G1TBM0_9BACT Unreviewed; 264 AA.
AC A0A0G1TBM0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00016014};
DE EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261};
GN ORFNames=UY05_C0038G0008 {ECO:0000313|EMBL:KKU79116.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWA2_47_7.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619058 {ECO:0000313|EMBL:KKU79116.1, ECO:0000313|Proteomes:UP000034737};
RN [1] {ECO:0000313|EMBL:KKU79116.1, ECO:0000313|Proteomes:UP000034737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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|ARBA:ARBA00002606}.
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|ARBA:ARBA00036072};
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000256|ARBA:ARBA00010699}.
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:KKU79116.1}.
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DR EMBL; LCON01000038; KKU79116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1TBM0; -.
DR PATRIC; fig|1619058.3.peg.438; -.
DR Proteomes; UP000034737; Unassembled WGS sequence.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.10.25.10; Formyl transferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
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; IPR044135; Met-tRNA-FMT_C.
DR InterPro; IPR041711; Met-tRNA-FMT_N.
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 {ECO:0000256|ARBA:ARBA00022917};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKU79116.1}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..264
FT /note="Methionyl-tRNA formyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002539764"
FT DOMAIN 8..119
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 167..263
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
SQ SEQUENCE 264 AA; 29807 MW; EEE5C3CFCFCDDF59 CRC64;
MSRLRLSVAF AGTPFFACPS LQALMMNPHF EVKMVITQPD KPVGRKYVLT ASPIKVLASK
NNIFIQQPEK ILDIKEEMVR LNPDFLIVVA YGKILPEELL TIPRFGAINV HASLLPKFRE
EDDTYLTLAE KLSVDSAQYL PQVLDDFAQG KIQAKPQDHA RATYCRKISK TDGLINFKTE
NAETIVRKIR AFTPWPGCFT FYKNKRIRIL SASVSEQKID TGKWLLIDKK TFGIGTKSGT
VLPLVVQPEG KKPMAVQDFI QGYF
//
