ID   TRMFO_ANADE             Reviewed;         450 AA.
AC   Q2ILE0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   10-JUN-2026, entry version 107.
DE   RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO {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 {ECO:0000255|HAMAP-Rule:MF_01037};
DE   AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037};
GN   Name=trmFO {ECO:0000255|HAMAP-Rule:MF_01037};
GN   OrderedLocusNames=Adeh_2697;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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; CP000251; ABC82467.1; -; Genomic_DNA.
DR   RefSeq; WP_011421749.1; NC_007760.1.
DR   AlphaFoldDB; Q2ILE0; -.
DR   SMR; Q2ILE0; -.
DR   STRING; 290397.Adeh_2697; -.
DR   KEGG; ade:Adeh_2697; -.
DR   eggNOG; COG1206; Bacteria.
DR   HOGENOM; CLU_033057_1_0_7; -.
DR   OrthoDB; 9803114at2; -.
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; Transferase;
KW   tRNA processing.
FT   CHAIN           1..450
FT                   /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT                   methyltransferase TrmFO"
FT                   /id="PRO_0000346317"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
SQ   SEQUENCE   450 AA;  48369 MW;  C5C2BE25A871FDDD CRC64;
     MGDTRVTVIG GGLAGSEAAW QLARAGVAVE LVEMKPERRS PAHVLPGLAE LVCSNSLRSD
     NPQNAVGLLH EELRRLGSLV LGCADATRVP AGDALAVDRE RFSEAVTARL SGHPGVRIVH
     REVEDLPPPP ALAVIATGPL TGDALAARLA EATGGRLHFY DAIAPIVAAE SIDRSIAYAR
     SRYGKGSGDD YLNLPLDEAQ YHAFVDALLQ GEKVPAHGFE EPRYFEGCLP IEVMAERGTE
     VLAHGPLKPV GLEDPRTGRW PHAVVQLRRE DVEGTAWNLV GFQTRLTWPE QRRIFRAFLP
     GLANAEFVRL GQIHRNTFVD APRVLAPDLS VRAAPHLFLA GQITGVEGYV ESAACGLMAA
     RAVLDRLAER AFRPPPAATA LGALHRHLTG EAHPPGYDYQ PSNVVFALFP PLTGRHRGKA
     GRKEAHVERA RKELAPWIDT APPPAVPAAG
//