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Database: UniProt
Entry: A0A669EBD8_ORENI
LinkDB: A0A669EBD8_ORENI
Original site: A0A669EBD8_ORENI 
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
//
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