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 01-MAY-2013, entry version 40.
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 + uridine(54)
CC in tRNA + FADH(2) = tetrahydrofolate + 5-methyluridine(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 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:HAMAP.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:HAMAP.
DR GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:EC.
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; 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 1 434 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
//
