ID   TMFO1_MYCCT             Reviewed;         438 AA.
AC   Q2SS13;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   10-JUN-2026, entry version 113.
DE   RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO 1 {ECO:0000255|HAMAP-Rule:MF_01037};
DE            EC=2.1.1.74 {ECO:0000255|HAMAP-Rule:MF_01037};
DE   AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01037};
DE   AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01037};
GN   Name=trmFO1 {ECO:0000255|HAMAP-Rule:MF_01037};
GN   OrderedLocusNames=MCAP_0476;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Mycoplasmataceae;
OC   Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-uridine
CC       at position 54 (M-5-U54) in all tRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_01037}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(54) in tRNA + (6R)-5,10-methylene-5,6,7,8-
CC         tetrahydrofolate + NADH + H(+) = 5-methyluridine(54) in tRNA + (6S)-
CC         5,6,7,8-tetrahydrofolate + NAD(+); Xref=Rhea:RHEA:16873, Rhea:RHEA-
CC         COMP:10167, Rhea:RHEA-COMP:10193, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15636, ChEBI:CHEBI:57453, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.74;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01037};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(54) in tRNA + (6R)-5,10-methylene-5,6,7,8-
CC         tetrahydrofolate + NADPH + H(+) = 5-methyluridine(54) in tRNA + (6S)-
CC         5,6,7,8-tetrahydrofolate + NADP(+); Xref=Rhea:RHEA:62372, Rhea:RHEA-
CC         COMP:10167, Rhea:RHEA-COMP:10193, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15636, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.74;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01037};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01037};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01037}.
CC   -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01037}.
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DR   EMBL; CP000123; ABC01640.1; -; Genomic_DNA.
DR   RefSeq; WP_011387349.1; NC_007633.1.
DR   AlphaFoldDB; Q2SS13; -.
DR   SMR; Q2SS13; -.
DR   GeneID; 23778568; -.
DR   KEGG; mcp:MCAP_0476; -.
DR   HOGENOM; CLU_033057_1_0_14; -.
DR   PhylomeDB; Q2SS13; -.
DR   BRENDA; 2.1.1.190; 3523.
DR   BRENDA; 2.1.1.B117; 3523.
DR   Proteomes; UP000001928; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047151; F:tRNA (uracil(54)-C5)-methyltransferase activity, 5,10-methylenetetrahydrofolate-dependent; IEA:UniProtKB-UniRule.
DR   GO; GO:0030488; P:tRNA methylation; IEA:TreeGrafter.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:TreeGrafter.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   HAMAP; MF_01037; TrmFO; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR040131; MnmG_N.
DR   InterPro; IPR004417; TrmFO.
DR   NCBIfam; TIGR00137; gid_trmFO; 1.
DR   NCBIfam; NF003739; PRK05335.1; 1.
DR   PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR   PANTHER; PTHR11806:SF2; METHYLENETETRAHYDROFOLATE--TRNA-(URACIL-5-)-METHYLTRANSFERASE TRMFO; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Methyltransferase; NAD; NADP;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..438
FT                   /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT                   methyltransferase TrmFO 1"
FT                   /id="PRO_0000346362"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
SQ   SEQUENCE   438 AA;  49833 MW;  B2D86B36DA32AFE9 CRC64;
     MNKKVKIIGA GLAGCEAAYF LANNDIQVEL YEVKTLIKNE VQKTNNFAEL VCSNTFRSQS
     LLNAAGILKA EMRRLNSLVI KIADSCKIDG DDALAVDRED FSKKLTDVIK NHPNITIIEQ
     NVSYIDDEND LTLIATGPLT TNELKEDIQR LIGKQKLFFM DASAPIITKD SIDFNKVYYS
     GRHKQGKYIC CPLNEQEFNK FVDDLVNAEQ VQLKEFEKSI FFKGCQPIEQ LAKTSKKLLL
     KGPMSPNNLL DQNNQQPYAV VQLRQDDAKD SLYNMVGFQT NLKWPEQKRV FQTIPGLEKA
     KIVRYGVMHK NYYINSPKIL NFKLQVIRKK NVFFAGQITG VEGYIESASS GIWAAINILA
     FINNKKIKPL PNTTILGALT NYITNSKIYS LKPMKCNLGI LEQENKYQSN DKFYSYNNSK
     NSLENYIEQL NKILRTNI
//