ID A0A669EBD8_ORENI Unreviewed; 393 AA.
AC A0A669EBD8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=Methionyl-tRNA formyltransferase, mitochondrial {ECO:0000256|ARBA:ARBA00014185};
DE EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261};
GN Name=MTFMT {ECO:0000313|Ensembl:ENSONIP00000070073.1};
GN Synonyms=mtfmt {ECO:0000313|Ensembl:ENSONIP00000070073.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000070073.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000070073.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSONIP00000070073.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Methionyl-tRNA formyltransferase that formylates methionyl-
CC tRNA in mitochondria and is crucial for translation initiation.
CC {ECO:0000256|ARBA:ARBA00057846}.
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|ARBA:ARBA00052555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24381;
CC Evidence={ECO:0000256|ARBA:ARBA00052555};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000256|ARBA:ARBA00010699}.
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DR AlphaFoldDB; A0A669EBD8; -.
DR Ensembl; ENSONIT00000080795.1; ENSONIP00000070073.1; ENSONIG00000014631.2.
DR GeneTree; ENSGT00390000017828; -.
DR InParanoid; A0A669EBD8; -.
DR Proteomes; UP000005207; Linkage group LG1.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR FunFam; 3.40.50.12230:FF:000003; methionyl-tRNA formyltransferase, mitochondrial; 1.
DR Gene3D; 3.40.50.12230; -; 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; 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; SSF53328; Formyltransferase; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 117..217
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 241..321
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
SQ SEQUENCE 393 AA; 44434 MW; 91A316568FF08DE7 CRC64;
MWTNAKTIRA YVETLKRCQR CCMGTLWRGD TDRGKRQLCR VLSSTSKPKW RLLFFGTDHF
AVESLKLLTS CRSTSEGIVE TLEVVTLAGD VPVKRFAQEN HLPLHSWPPD DVNGRFDVGV
VVSFGCLLPE RLIRKFPYGI LNVHPSLLPR WRGPAPVFHT ILHGDSVTGV SIIQIRPHRF
DVGPILNQQL YQVPENCTAD ELGGTLATMG AHLLIKTLMS LSERMENQRE QGQTGATFAP
KIKTSMSWIV WEEQTCDQID RLYRAVGSRI PLRTMWMGRT IKLLDFTGKC HVSLSDQRRN
PIPGSVSFQK DSNTLAVCCK VGPTVPSSTP DLLYCMLTIA SELFLSFSTE VIGDFHTVAT
IAKQHIKDIV FVQINWMVQL NVRPCWRYFS TLL
//