ID A0A4Z0Q400_9BACT Unreviewed; 313 AA.
AC A0A4Z0Q400;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 02-APR-2025, entry version 19.
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=E5K00_01100 {ECO:0000313|EMBL:TGE23843.1};
OS Hymenobacter aquaticus.
OC Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC Hymenobacteraceae; Hymenobacter.
OX NCBI_TaxID=1867101 {ECO:0000313|EMBL:TGE23843.1, ECO:0000313|Proteomes:UP000297549};
RN [1] {ECO:0000313|EMBL:TGE23843.1, ECO:0000313|Proteomes:UP000297549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 31653 {ECO:0000313|EMBL:TGE23843.1,
RC ECO:0000313|Proteomes:UP000297549};
RA Feng G., Zhang J., Zhu H.;
RL Submitted (APR-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:TGE23843.1}.
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DR EMBL; SRLC01000001; TGE23843.1; -; Genomic_DNA.
DR RefSeq; WP_135460828.1; NZ_SRLC01000001.1.
DR AlphaFoldDB; A0A4Z0Q400; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000297549; 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:UP000297549};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 3..179
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 205..304
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT BINDING 110..113
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 313 AA; 33639 MW; B6F9BE7F679A4DF1 CRC64;
MLRIVFMGTP EFAVPTLETL LTWSGCEVVA VITAPDKPAG RGRQLAESAV KQAAAAHGLP
VLQPTNLKAP EFQQELRGYA ADLQVVVAFR MLPEAVWNMP RLGSINIHAS LLPQYRGAAP
INWALIQGEK QTGVTSFFLQ HEIDTGNLIF QDVVPIADDD DFGALYEKLK AAGARLALRT
VQAIAAGTAP SIPQTTGQEL KSAPKIQKET GRLDAAQPAA ALVNLVRGLS PIPTAFTQLP
DGRTLKIFKA KALDETKPAA PGTWATDGRT YLRLHTGQGQ LDLLDVQLEG KKRMPVVEFL
RGFNAAVLNA PTV
//
