ID C6XJ10_HIRBI Unreviewed; 473 AA. AC C6XJ10; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 87. 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=Hbal_1414 {ECO:0000313|EMBL:ACT59105.1}; OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales; OC Hyphomonadaceae; Hirschia. OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT59105.1, ECO:0000313|Proteomes:UP000002745}; RN [1] {ECO:0000313|Proteomes:UP000002745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418 RC {ECO:0000313|Proteomes:UP000002745}; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). 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; CP001678; ACT59105.1; -; Genomic_DNA. DR RefSeq; WP_015827255.1; NC_012982.1. DR AlphaFoldDB; C6XJ10; -. DR STRING; 582402.Hbal_1414; -. DR KEGG; hba:Hbal_1414; -. DR eggNOG; COG1206; Bacteria. DR HOGENOM; CLU_033057_1_0_5; -. DR OrthoDB; 9803114at2; -. DR Proteomes; UP000002745; 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; 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 PRINTS; PR00411; PNDRDTASEI. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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:UP000002745}; 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 17..388 FT /note="MnmG N-terminal" FT /evidence="ECO:0000259|Pfam:PF01134" FT REGION 438..459 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 21..26 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01037" SQ SEQUENCE 473 AA; 51831 MW; E7CC48318D4ADC3A CRC64; MTQLDNDANQ KSTLAPIHVI GGGMAGCEAA WQAANLGVPV ILHEMRPTKK TEAHQTDGLA ELVCSNSFRS DDFENNAVGL LHEEMRRANG LIISTAHDHQ IPAGSALAVD RDGFSQAVTA KIQAHPLITI EREEVPGIPP AEWDSVIIAT GPLTSPSMGE AIKELTGEDE LSFFDAIAPI VYYDSIDMSK AWRQSRYDKP GPSGETDAYV NCPMNEEQYL AFLEALNNAP KTEFKEWEKD TPYFEGCLPV EVMASRGPET LRYGPLKPVG LTNAHQPDVK AHAIVQLRQD NKLGTLWNIV GFQTKMTYGA QKDVLRMIPG LENAEFARLG GIHRNTFINS PKVLNNKLQL KNQLRIRFAG QVSGVEGYVE SAAMGLLAGR FAAFERLGRE ISPPPETTAL GSLISHVTGG HLIGKATFQP MNVNFGLFPD IDFAKADPET GKRYRGKDKS RAKKRAQSAR ALKDIQEWLG TQS //