ID TRMFO_STRU0 Reviewed; 444 AA.
AC B9DS62;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 29-MAY-2013, entry version 35.
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=SUB0921;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A.,
RA Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A.,
RA Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N.,
RA Whatmore A.M., Bentley S.D., Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR42047.1; -; Genomic_DNA.
DR RefSeq; YP_002562247.1; NC_012004.1.
DR ProteinModelPortal; B9DS62; -.
DR STRING; 218495.SUB0921; -.
DR EnsemblBacteria; CAR42047; CAR42047; SUB0921.
DR GeneID; 7391394; -.
DR KEGG; sub:SUB0921; -.
DR PATRIC; 19807538; VBIStrUbe20775_0889.
DR eggNOG; COG1206; -.
DR HOGENOM; HOG000252054; -.
DR KO; K04094; -.
DR OMA; RFAGQIT; -.
DR ProtClustDB; PRK05335; -.
DR BioCyc; SUBE218495:GJ7D-959-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 1 444 Methylenetetrahydrofolate--tRNA-(uracil-
FT 5-)-methyltransferase TrmFO.
FT /FTId=PRO_1000149479.
FT NP_BIND 10 15 FAD (By similarity).
SQ SEQUENCE 444 AA; 49211 MW; B66A7FE7F52C9647 CRC64;
MSQSYINVIG AGLAGSEAAY QIAKRGIPVK LYEMRGVKAT PQHKTSNFAE LVCSNSFRGD
SLTNAVGLLK EEMRRLDSII MRAGEAHRVP AGGAMAVDRV GYAEAVTAEL ENNPLIEVIR
GEITEIPNDA ITVIATGPLT SDALAEKIHA LNGGEGFYFY DAAAPIIDKS TINMDKVYLK
SRYDKGEAAY LNCPMTKEEF LAFHEALTTA EEAPLNSFEK EKYFEGCMPI EVMAKRGIKT
MLYGPMKPVG LEYPDDYKGP RDGDYKTPYA VVQLRQDNAA GSLYNMVGFQ THLKWGEQKR
VFQMIPGLEN AEFVRYGVMH RNSYMDSPNL LKQTFQSRAN ENLFFAGQMT GVEGYVESAA
SGLVAGINAA RLFKGEEAII FPETTAIGSL PHYVTHTDSK HFQPMNVNFG IIKELEGKRI
RDKKERYEAI AERSLKDLEA FLNS
//
