ID   TRMFO_LACS1             Reviewed;         436 AA.
AC   Q1WU04;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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; Synonyms=gid; OrderedLocusNames=LSL_0721;
OS   Lactobacillus salivarius subsp. salivarius (strain UCC118).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C.,
RA   Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F.,
RA   van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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.
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DR   EMBL; CP000233; ABD99531.1; -; Genomic_DNA.
DR   RefSeq; YP_535614.1; -.
DR   GeneID; 3976950; -.
DR   GenomeReviews; CP000233_GR; LSL_0721.
DR   KEGG; lsl:LSL_0721; -.
DR   HOGENOM; Q1WU04; -.
DR   OMA; Q1WU04; MKPVGLT.
DR   BioCyc; LSAL362948:LSL_0721-MON; -.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW   Transferase; tRNA processing.
FT   CHAIN         1    436       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase trmFO.
FT                                /FTId=PRO_1000072978.
FT   NP_BIND       9     14       FAD (By similarity).
SQ   SEQUENCE   436 AA;  48676 MW;  01571FADDDE6DB3C CRC64;
     MTASVNVIGA GLAGSEAAWQ IANQGVKVRL YEMRPQKLTP AHHNENFAEL VCTNSLRANR
     LTNAAGLLKE EMRTFNSIIM ESADKHSVPA GGALAVDRET FSKEVTEKLH NHPNVEIINE
     EIDEIPEGLT VIATGPLTSD ALAKDITKFT GSDGLFFFDA AAPILEKSSL DMDKVYLKSR
     YDKGEAAYLN APMTKDEFYN FYNELIKAET AELHDFEDDK FFEGCMPIEE IASRGAQTML
     YGPLKPVGLE DPRTGKEPFA VVQLRQDNAA GDLYNIVGFQ THLKWGEQKR VFSMIPGLEN
     ARFVRYGVMH RNTFLCSPEV MQATYQTKKR LDLFFAGQMT GVEGYVESAA SGLYAGLNAA
     RIAQGKDPVI FPEETMMGAM AHYITHASVK NFQPINANFG IVPKLQERIR NKQERNLKIS
     ERAIDRIKKF KNLNFD
//