ID   TRMFO_FERNB             Reviewed;         430 AA.
AC   A7HL16;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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}; OrderedLocusNames=Fnod_0744;
OS   Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=381764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL   Submitted (JUL-2007) 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=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH +
CC         uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC         methyluridine(54) in tRNA + 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=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH +
CC         uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC         methyluridine(54) in tRNA + 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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000771; ABS60599.1; -; Genomic_DNA.
DR   RefSeq; WP_011993917.1; NC_009718.1.
DR   AlphaFoldDB; A7HL16; -.
DR   SMR; A7HL16; -.
DR   STRING; 381764.Fnod_0744; -.
DR   EnsemblBacteria; ABS60599; ABS60599; Fnod_0744.
DR   KEGG; fno:Fnod_0744; -.
DR   eggNOG; COG1206; Bacteria.
DR   HOGENOM; CLU_033057_1_0_0; -.
DR   OMA; MHRNTFL; -.
DR   OrthoDB; 516534at2; -.
DR   Proteomes; UP000002415; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030698; F:5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; -; 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   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF2; PTHR11806:SF2; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00137; gid_trmFO; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Methyltransferase; NAD; NADP;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..430
FT                   /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT                   methyltransferase TrmFO"
FT                   /id="PRO_0000346340"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
SQ   SEQUENCE   430 AA;  48310 MW;  3062B7A89AE768F7 CRC64;
     MNKLVHIIGA GLAGSEAAWQ LVKNGFNVVI HEMKRVKKSP VHVSENFAEL VCSNSLKSTD
     LKNAEGLLKA EMEIWGSLIL ECAYNNSVPA GKALAVDREK FSQCVTEKLL QTGLVKVVWE
     EVEKPYTDDI WIIATGPTTD GKLAEWIREQ TGGFFNFFDA VAPIVSAESI NMDVCFVADR
     YGVGTGDYIN CPMTKEEYER FWNELVNAQV IEIEDFDRKL LFERCQPIEE IARSGKDAMR
     YGPLRPVGIV DPKTGKEPYA VIQLRKENVE GTMYNIVGFQ TRLKWGEQRR IIQLIPGLEN
     AEILRYGVMH RNSYIDSPKV LDEYLRLKKM PNVFFAGQIT GVEGYVESAM TGLYVGLNIS
     RLILGKDMIK FPEKTMCGAL VRYITTAPEL KPMYANFGLL GGGKDREKIA LKALDEMKKF
     YQITSLTIGG