ID B8DG55_LISMH Unreviewed; 434 AA.
AC B8DG55;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 31.
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=LMHCC_1300;
OS Listeria monocytogenes serotype 4a (strain HCC23).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=552536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCC23;
RX PubMed=21602330; DOI=10.1128/JB.05236-11;
RA Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T.,
RA Bridges S.M., Lawrence M.L.;
RT "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK39645.1; -; Genomic_DNA.
DR RefSeq; YP_002350259.1; NC_011660.1.
DR ProteinModelPortal; B8DG55; -.
DR STRING; 552536.LMHCC_1300; -.
DR EnsemblBacteria; ACK39645; ACK39645; LMHCC_1300.
DR GeneID; 7080230; -.
DR KEGG; lmh:LMHCC_1300; -.
DR PATRIC; 20317713; VBILisMon86872_1287.
DR eggNOG; COG1206; -.
DR HOGENOM; HOG000252054; -.
DR KO; K04094; -.
DR OMA; RFAGQIT; -.
DR ProtClustDB; PRK05335; -.
DR BioCyc; LMON552536:GIW4-1333-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; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW Transferase; tRNA processing.
FT NP_BIND 9 14 FAD (By similarity).
SQ SEQUENCE 434 AA; 47851 MW; DAA870400DF43EAA CRC64;
MEKSVNVIGA GLAGSEAAWQ LVKRGVKVDL YEMRPVKQTP AHHTDKFAEL VCTNSLRANG
LTNAVGVIKE EMRILDSIII EAADKASVPA GGALAVDRHE FSGYITDKVK NHPLVTVHTE
EVTTIPEGPT IIATGPLTSP ALADEIKQLT GEEYLYFYDA AAPIIEKDSI DMDKVYLKSR
YDKGEAAYLN CPMSEEEFNA FYEALVTAET AALKEFEKEV FFEGCMPIEV MAKRGIKTML
FGPLKPVGLE DPKTGKRPYA VLQLRQDDAA GTLYNMVGFQ THLKWGEQKR VFGMIPGLEN
AEIVRYGVMH RNTFINSPTV LEPTYQLKTR NDLFFAGQMT GVEGYVESAA SGLAAGINAA
NFVEEKELVV FPAETAIGSL AHYITSASKK SFQPMNVNFG LFPELETKIR AKQERNEKLA
ERALNAIKRV AEQL
//
