ID   FMT_BOVIN               Reviewed;         390 AA.
AC   O77480;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Methionyl-tRNA formyltransferase, mitochondrial;
DE            Short=MtFMT;
DE            EC=2.1.2.9 {ECO:0000269|PubMed:9614118};
DE   Flags: Precursor;
GN   Name=MTFMT; Synonyms=FMT;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 19-390, PROTEIN SEQUENCE OF 34-40; 86-95 AND
RP   195-204, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Heart, and Liver;
RX   PubMed=9614118; DOI=10.1074/jbc.273.24.15085;
RA   Takeuchi N., Kawakami M., Omori A., Ueda T., Spremulli L.L., Watanabe K.;
RT   "Mammalian mitochondrial methionyl-tRNA transformylase from bovine liver.
RT   Purification, characterization, and gene structure.";
RL   J. Biol. Chem. 273:15085-15090(1998).
CC   -!- FUNCTION: Methionyl-tRNA formyltransferase that formylates methionyl-
CC       tRNA in mitochondria and is crucial for translation initiation.
CC       {ECO:0000269|PubMed:9614118}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-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:57454,
CC         ChEBI:CHEBI:78530, ChEBI:CHEBI:78844; EC=2.1.2.9;
CC         Evidence={ECO:0000269|PubMed:9614118};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24381;
CC         Evidence={ECO:0000305|PubMed:9614118};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.025 uM for L-methionyl-tRNA(fMet) {ECO:0000269|PubMed:9614118};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9614118}.
CC   -!- DOMAIN: Composed of an N- and a C-terminal domain. The N-terminal
CC       domain carries the tetrahydrofolate (THF)-binding site and the C-
CC       terminal domain is presumably involved in positioning the Met-tRNA
CC       substrate for the formylation reaction.
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}.
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DR   EMBL; AB004316; BAA31237.1; -; mRNA.
DR   RefSeq; NP_001159995.1; NM_001166523.1.
DR   AlphaFoldDB; O77480; -.
DR   SMR; O77480; -.
DR   STRING; 9913.ENSBTAP00000028820; -.
DR   PaxDb; O77480; -.
DR   PRIDE; O77480; -.
DR   Ensembl; ENSBTAT00000028820; ENSBTAP00000028820; ENSBTAG00000021630.
DR   GeneID; 286855; -.
DR   KEGG; bta:286855; -.
DR   CTD; 123263; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021630; -.
DR   VGNC; VGNC:31724; MTFMT.
DR   eggNOG; KOG3082; Eukaryota.
DR   GeneTree; ENSGT00390000017828; -.
DR   HOGENOM; CLU_033347_0_0_1; -.
DR   InParanoid; O77480; -.
DR   OMA; FMPELHA; -.
DR   OrthoDB; 963177at2759; -.
DR   TreeFam; TF323405; -.
DR   SABIO-RK; O77480; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000021630; Expressed in oocyte and 103 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; IDA:UniProtKB.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 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; IPR041711; Met-tRNA-FMT_N.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF50486; SSF50486; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00460; fmt; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Mitochondrion; Protein biosynthesis;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305|PubMed:9614118"
FT   CHAIN           34..390
FT                   /note="Methionyl-tRNA formyltransferase, mitochondrial"
FT                   /id="PRO_0000010092"
FT   CONFLICT        20..22
FT                   /note="RRS -> TRP (in Ref. 2; BAA31237)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   390 AA;  43620 MW;  D92E740B5F465FFE CRC64;
     MRVLLRCCCG HLPVGGGAGR RSNPRWRALA RLSASPGWED GQGARVREKP PWRVLFFGND
     QFARETLRAL HAARENKEEE LIEKLEVVTV PSPSPKGLPV KQYAVQSQLP VYEWPDVGSG
     EYDVGVVASF GRLLSEAFIL KFPYGILNVH PSCLPRWRGP APIIHTILHG DTIAGVTIMQ
     IKPRRFDVGP ILKQETVPVP PKSTSKELEA VLSRLGANML ISVLKNLPES LNNGRQQPAE
     GVTHAPKISA ATSCIKWEEQ TSEQIFRLYR AVGNIIPLQT LWMDNTIKLL DLVEVDNSIL
     SDSKLTGQAV IPGSVIYHKQ SQILLVCCKD DWIGVRSVML KKTLTATDFY NGYLHPWYQK
     NSQAQPSQCR FQTLRLPPKK KQKKKIVAMQ