ID TRMFO_STRA5 Reviewed; 444 AA. AC Q8DZX5; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 111. 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}; Synonyms=gid; GN OrderedLocusNames=SAG0969; OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=208435; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-611 / 2603 V/R; RX PubMed=12200547; DOI=10.1073/pnas.182380799; RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N., RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D., RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D., RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A., RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T., RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.; RT "Complete genome sequence and comparative genomic analysis of an emerging RT human pathogen, serotype V Streptococcus agalactiae."; RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002). 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; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE009948; AAM99853.1; -; Genomic_DNA. DR RefSeq; NP_687981.1; NC_004116.1. DR RefSeq; WP_000083750.1; NC_004116.1. DR AlphaFoldDB; Q8DZX5; -. DR SMR; Q8DZX5; -. DR STRING; 208435.SAG0969; -. DR KEGG; sag:SAG0969; -. DR PATRIC; fig|208435.3.peg.975; -. DR HOGENOM; CLU_033057_1_0_9; -. DR OrthoDB; 9803114at2; -. DR Proteomes; UP000000821; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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-EC. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule. 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; IPR020595; MnmG-rel_CS. DR InterPro; IPR040131; MnmG_N. DR InterPro; IPR004417; TrmFO. DR NCBIfam; TIGR00137; gid_trmFO; 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. DR PROSITE; PS01281; GIDA_2; 1. PE 3: Inferred from homology; KW Cytoplasm; FAD; Flavoprotein; Methyltransferase; NAD; NADP; KW Reference proteome; Transferase; tRNA processing. FT CHAIN 1..444 FT /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)- FT methyltransferase TrmFO" FT /id="PRO_0000117270" FT BINDING 10..15 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01037" SQ SEQUENCE 444 AA; 49511 MW; CA438676C26001C4 CRC64; MSQSYINVIG AGLAGSEAAY QIAKRGIPVK LYEMRGVKST PQHKTDNFAE LVCSNSFRGD SLTNAVGLLK EEMRRLDSII MRNGEAHRVP AGGAMAVDRE GYSEAVTEEI HKHPLIEVIR DEITDIPGDA ITVIATGPLT SDSLAAKIHE LNGGDGFYFY DAAAPIVDKN TIDINKVYLK SRYDKGEAAY LNCPMTKEEF MAFHEALTTA EEAPLNSFEK EKYFEGCMPI EVMAKRGIKT MLYGPMKPVG LEYPEDYKGP RDGEFKTPYA VVQLRQDNAA GSLYNIVGFQ THLKWGEQKR VFQMIPGLEN AEFVRYGVMH RNSYMDSPNL LNQTFATRKN PNLFFAGQMT GVEGYVESAA SGLVAGINAV RRFNGESEVV FPQTTAIGAL PHYITHTDSK HFQPMNVNFG IIKELEGPRI RDKKERYEAI ATRALKDLEK FLNY //