ID   TRMFO_ANAD2             Reviewed;         453 AA.
AC   B8JES4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=A2cp1_2883;
OS   Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=455488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-1 / ATCC BAA-258;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Beliaev A.S., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL   Submitted (JAN-2009) 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; CP001359; ACL66220.1; -; Genomic_DNA.
DR   RefSeq; WP_012633969.1; NC_011891.1.
DR   AlphaFoldDB; B8JES4; -.
DR   SMR; B8JES4; -.
DR   EnsemblBacteria; ACL66220; ACL66220; A2cp1_2883.
DR   KEGG; acp:A2cp1_2883; -.
DR   HOGENOM; CLU_033057_1_0_7; -.
DR   OMA; MHRNTFL; -.
DR   Proteomes; UP000007089; 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; Transferase;
KW   tRNA processing.
FT   CHAIN           1..453
FT                   /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT                   methyltransferase TrmFO"
FT                   /id="PRO_1000149462"
FT   REGION          433..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
SQ   SEQUENCE   453 AA;  48626 MW;  FD829B833C6A35ED CRC64;
     MGDTRVTVIG GGLAGTEAAW QLARAGVAVE LVEMKPERRS PAHVLPGLAE LVCSNSLRSD
     NPLNAVGLLH EELRRLGSLV LGCADETRVP AGDALAVDRE RFSEAVTARL TGHAGVRIVH
     RELEELPPPP ALAVIATGPL TADALAARLA ETTGGRLHFY DAIAPIVAAE SIDRSIAYAR
     SRYGKGSGDD YLNLPLDEAQ YHAFVEALLQ GEKVAAHGFE EPRYFEGCLP IEVMAERGLE
     VLAHGPLKPV GLEDPRTGRR PHAVVQLRRE DVDGTAWNLV GFQTRLTWPE QRRIFRAFLP
     GLANAEFVRL GQIHRNTFVD APRVLAPDLS VRAAPHLFLA GQITGVEGYV ESAACGLMAA
     RAVLDRLAGR AFRPPPPATA LGALHRHLTG EAHPPGYDYQ PSNVVFALFP PLTGRHRGKA
     GRKEAHVERA RKELAPWIDS APPTAVPAAP AAG