ID E6TSX6_EVAC2 Unreviewed; 434 AA. AC E6TSX6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 71. DE RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO {ECO:0000256|HAMAP-Rule:MF_01037}; DE EC=2.1.1.74 {ECO:0000256|HAMAP-Rule:MF_01037}; DE AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01037}; DE AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01037}; GN Name=trmFO {ECO:0000256|HAMAP-Rule:MF_01037}; GN OrderedLocusNames=Bcell_2511 {ECO:0000313|EMBL:ADU30768.1}; OS Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM OS 9156 / N-4) (Bacillus cellulosilyticus). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Evansella. OX NCBI_TaxID=649639 {ECO:0000313|EMBL:ADU30768.1, ECO:0000313|Proteomes:UP000001401}; RN [1] {ECO:0000313|EMBL:ADU30768.1, ECO:0000313|Proteomes:UP000001401} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4 RC {ECO:0000313|Proteomes:UP000001401}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Brumm P., Mead D., RA Woyke T.; RT "Complete sequence of Bacillus cellulosilyticus DSM 2522."; RL Submitted (DEC-2010) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01037}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, ECO:0000256|HAMAP- CC Rule:MF_01037}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01037}. CC -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily. CC {ECO:0000256|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; CP002394; ADU30768.1; -; Genomic_DNA. DR AlphaFoldDB; E6TSX6; -. DR STRING; 649639.Bcell_2511; -. DR KEGG; bco:Bcell_2511; -. DR eggNOG; COG1206; Bacteria. DR HOGENOM; CLU_033057_1_0_9; -. DR Proteomes; UP000001401; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01037}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01037}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_01037}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_01037}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01037}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01037}; KW Reference proteome {ECO:0000313|Proteomes:UP000001401}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01037}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_01037}. FT DOMAIN 5..367 FT /note="MnmG N-terminal" FT /evidence="ECO:0000259|Pfam:PF01134" FT BINDING 9..14 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01037" SQ SEQUENCE 434 AA; 48678 MW; 7D1F584A608BDA37 CRC64; MTQHVNVIGA GLAGSEAAWQ IAKRGIPVHL YEMRPKKQTP AHHTDKFAEL VCSNSLRANT LTNAVGVLKE EMRILDSVII QSADDCSVPA GGALAVDRHE FAALVTERVK NHELVTVFED EVTEIPEGPT IICTGPLTSE SLSHRLKELT GEEYLYFYDA AAPIIDADSI DRNKVYLKSR YDKGEAAYLN CPMTEEEFNT FYDALIEAET VPVKEFEKEM FFEGCMPVEV MAKRGRKTLL FGPMKPVGLE DPKTNKRPFA VVQLRQDNSS GTLFNIVGFQ THMKWGPQKE VIQLIPGLEN AEIVRFGVMH RNTFINSPNL LKPTYQYRDR DDLFFAGQMT GVEGYVESAA AGLVAGINAS RLIQEKETVT FPNETVIGSM AQYITTANHK NFQPMNANFG LLPPFEQRIK NKQERNEKHA NRALETIQNF VKKM //