ID   TRMFO_PARMW             Reviewed;         461 AA.
AC   Q7U7T2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=SYNW0899;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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; BX569691; CAE07414.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7U7T2; -.
DR   SMR; Q7U7T2; -.
DR   STRING; 84588.SYNW0899; -.
DR   EnsemblBacteria; CAE07414; CAE07414; SYNW0899.
DR   KEGG; syw:SYNW0899; -.
DR   eggNOG; COG1206; Bacteria.
DR   HOGENOM; CLU_033057_1_0_3; -.
DR   OMA; MHRNTFL; -.
DR   Proteomes; UP000001422; 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..461
FT                   /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT                   methyltransferase TrmFO"
FT                   /id="PRO_0000346412"
FT   BINDING         16..21
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
SQ   SEQUENCE   461 AA;  50688 MW;  F9C6FDFE3C9975EC CRC64;
     MLQLLLSVER PVTVLGAGLA GTEAAWQVAR AGIPVTIVEM RPMRRSPAHH SSDFAELVCS
     NSFGALSSDR AAGLLQEEMR RLGSLVIETA DAHAVPAGGA LAVDRGRYSA ALTEALDQHP
     LVTIERREQQ ALPGDDQITV LATGPLTSEP LAEDLRAFTG RSDCHFFDAA SPIVHGDSID
     LNVAFRASRY DKGDADYINC PMDKEQYLAF REALLTAEQA ELKDFDKNDA TFFEGCLPIE
     ELARRGEDTM RYGPLKPIGL WDPRWGDVND RDVRRAKRAY AVVQLRQEDK DGRLWNLVGF
     QTNLKWGEQK RVLQMIPGLA EAEFVRFGVM HRNTFLESPQ LLEPTLQFRS RSSLLAAGQI
     TGTEGYAAAV AGGWLAGTNA ARLARGLAPI DLPATCMSGA LTHFVSEAPT AKFQPMPPNF
     GLLPELPERI RDKRARYGAY RDRALRDLER IKALTPNALV A