ID A0A7C9B916_9BACT Unreviewed; 299 AA.
AC A0A7C9B916;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 02-APR-2025, entry version 15.
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=GBK04_06860 {ECO:0000313|EMBL:MPR33082.1};
OS Salmonirosea aquatica.
OC Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC Spirosomataceae; Salmonirosea.
OX NCBI_TaxID=2654236 {ECO:0000313|EMBL:MPR33082.1, ECO:0000313|Proteomes:UP000479293};
RN [1] {ECO:0000313|EMBL:MPR33082.1, ECO:0000313|Proteomes:UP000479293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJW1-29 {ECO:0000313|EMBL:MPR33082.1,
RC ECO:0000313|Proteomes:UP000479293};
RA Choi A.;
RT "Draft Genome Sequence of Cytophagaceae sp. SJW1-29.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
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=L-methionyl-tRNA(fMet) + (6R)-10-formyltetrahydrofolate = N-
CC formyl-L-methionyl-tRNA(fMet) + (6S)-5,6,7,8-tetrahydrofolate + H(+);
CC Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-COMP:9953,
CC 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|ARBA:ARBA00010699,
CC ECO:0000256|HAMAP-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:MPR33082.1}.
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; WHLY01000002; MPR33082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7C9B916; -.
DR Proteomes; UP000479293; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00182}; Reference proteome {ECO:0000313|Proteomes:UP000479293};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 4..173
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 199..298
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT BINDING 103..106
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 299 AA; 33481 MW; 8E88471392D91FFF CRC64;
MGTPEFAVSS LQLLLDNQCE VVAVITAPDR PAGRGQKLTE SPVKQCAVAR GIPVLQPEKL
KNPEFLATLR SFEADLQVVV AFRMLPEVVW AMPRLGTFNL HASLLPDYRG AAPINWAIMN
GETETGVTTF FIEKEIDTGK IIFQEKEAIA SDDTAGTLYE RLMKQGAQLV LRTVRAIEAG
TYPQIPQPAG REGKEAPKLF RETCEIDWNR PAAEIRNFVR GLSPYPAAWT TLNGQFCKLY
HVSVVKPDPE PNAEPGDYWS DQKTFLYFRA ADAWVAVHDI QVEGKKRMKT EDLLRGFRF
//
