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Database: UniProt
Entry: A9VT70
LinkDB: A9VT70
Original site: A9VT70 
ID   TRMFO_BACWK             Reviewed;         434 AA.
AC   A9VT70;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   19-FEB-2014, entry version 43.
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=BcerKBAB4_3655;
OS   Bacillus weihenstephanensis (strain KBAB4).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA   Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H.,
RA   Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(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 + uracil(54) in
CC       tRNA + FADH(2) = tetrahydrofolate + 5-methyluracil(54) in tRNA +
CC       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; CP000903; ABY44826.1; -; Genomic_DNA.
DR   RefSeq; YP_001646454.1; NC_010184.1.
DR   ProteinModelPortal; A9VT70; -.
DR   STRING; 315730.BcerKBAB4_3655; -.
DR   EnsemblBacteria; ABY44826; ABY44826; BcerKBAB4_3655.
DR   GeneID; 5843867; -.
DR   KEGG; bwe:BcerKBAB4_3655; -.
DR   PATRIC; 19011947; VBIBacWei55973_4290.
DR   eggNOG; COG1206; -.
DR   HOGENOM; HOG000252054; -.
DR   KO; K04094; -.
DR   OMA; RFAGQIT; -.
DR   OrthoDB; EOG6J74VT; -.
DR   ProtClustDB; PRK05335; -.
DR   BioCyc; BWEI315730:GHRU-3770-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030698; F:5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030488; P:tRNA methylation; IEA:GOC.
DR   HAMAP; MF_01037; TrmFO; 1.
DR   InterPro; IPR004417; Folate-dep_Ribothymidyl_synth.
DR   InterPro; IPR002218; GIDA-rel.
DR   InterPro; IPR020595; GIDA-rel_CS.
DR   Pfam; PF01134; GIDA; 1.
DR   TIGRFAMs; TIGR00137; gid_trmFO; 1.
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    434       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase TrmFO.
FT                                /FTId=PRO_0000346321.
FT   NP_BIND      10     15       FAD (By similarity).
SQ   SEQUENCE   434 AA;  48054 MW;  7F1F43650F6D8CF8 CRC64;
     MTTQVVNVIG AGLAGSEAAY QIAKRGVQVK LYEMRPVRQT PAHHTDKFAE LVCSNSLRAN
     TLTNAVGVIK EEMRLMDSVI IRAADECSVP AGGALAVDRH EFAAKVTEYV KNHPNVTVMN
     EEITEIPEGP TVIATGPLTS PDLSAQLKKL TGEDYFYFYD AAAPIVEKDS IDMNKVYLKS
     RYDKGEAAYL NCPMTEEEFD RFYEALIAAE TVPLKEFEKE IFFEGCMPVE VMASRGRQTL
     VFGPMKPVGL EDPKTGKTPY AVVQLRQDDA AGTLYNIVGF QTHLKWGPQK EVLQLIPGLE
     NAEIVRYGVM HRNTFINSPN LLRPTYQYKQ RDDLFFAGQM TGVEGYVESA ASGLLAGINA
     ARLVKGEEPV VLPPVTAMGS MANYITATNA KNFQPMNANF GLFTPLEKKI KKKQERNEAY
     ATRALETIQN FVNI
//
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