ID TRMFO_LACH4 Reviewed; 407 AA. AC A8YV48; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 16-JUN-2009, entry version 13. DE RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase trmFO; DE EC=2.1.1.74; DE AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase; DE AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase; GN Name=trmFO; OrderedLocusNames=lhv_1075; OS Lactobacillus helveticus (strain DPC 4571). OC Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=405566; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17993529; DOI=10.1128/JB.01295-07; RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K., RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F., RA Beresford T., Ross R.P.; RT "Genome sequence of Lactobacillus helveticus: an organism RT distinguished by selective gene loss and IS element expansion."; RL J. Bacteriol. 190:727-735(2008). CC -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl- CC uridine at position 54 (M-5-U54) in all tRNAs (By similarity). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + tRNA CC containing uridine at position 54 + FADH(2) = tetrahydrofolate + CC tRNA containing ribothymidine at position 54 + FAD. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the mnmG family. TrmFO subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000517; ABX27136.1; -; Genomic_DNA. DR RefSeq; YP_001577427.1; -. DR GeneID; 5771781; -. DR GenomeReviews; CP000517_GR; lhv_1075. DR KEGG; lhe:lhv_1075; -. DR OMA; A8YV48; MKPVGLT. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:FAD binding; IEA:HAMAP. DR GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-...; IEA:EC. DR GO; GO:0009021; F:tRNA (uracil-5-)-methyltransferase activity; IEA:HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:HAMAP. DR HAMAP; MF_01037; -; 1. DR InterPro; IPR004417; Gid. DR InterPro; IPR002218; GIDA-rel. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR11806; GIDA; 1. DR Pfam; PF01134; GIDA; 1. DR ProDom; PD003738; GIDA; 1. DR TIGRFAMs; TIGR00137; gid_trmFO; 1. DR PROSITE; PS01280; GIDA_1; FALSE_NEG. DR PROSITE; PS01281; GIDA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase; KW Transferase; tRNA processing. FT CHAIN 1 407 Methylenetetrahydrofolate--tRNA-(uracil- FT 5-)-methyltransferase trmFO. FT /FTId=PRO_0000346347. FT NP_BIND 9 14 FAD (By similarity). SQ SEQUENCE 407 AA; 44505 MW; F48EA9357797715A CRC64; MPKNVTVIGA GLAGSEATWQ LAKRGIHVDL YEMRPQKETP AHETGEFAEL VCTNSMRSNQ LSNAVGLLKE EMRHLDSLIM KAADKTQVPA GGALAVDRDS FSKYVTDTLR GLDNVTVHEE EITEIPEDGI TIIATGPLTS DALAEQIQKF SGTDSLHFFD AAAPIVAADS IDMNIVYKKS RYDRGEAAYL NCPMNKEQYE NFTRELIKAE TAQLHGFEKN DVFEGCMPIE VMAARGAKTM LFGPLKPVGL EDPHTGETPY AVVQLRQDNA AASMYNIVGF QTHLKYGEQK RVFSMIPGLE NARFVRYGKM HRNTYMASPD VLTASYEAKK RPGLFFAGQM TGVEGYVESA GSGLVAGVNA AREALGEEPI AFPKDTALGS MANYVTTTSA KHFPPMNASL HFYLLGK //