TRMFO_STRR6
ID TRMFO_STRR6 Reviewed; 444 AA.
AC Q8DQ51;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO {ECO:0000255|HAMAP-Rule:MF_01037};
DE EC=2.1.1.74 {ECO:0000255|HAMAP-Rule:MF_01037};
DE AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037};
DE AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037};
GN Name=trmFO {ECO:0000255|HAMAP-Rule:MF_01037}; Synonyms=gid;
GN OrderedLocusNames=spr0844;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
CC -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-uridine
CC at position 54 (M-5-U54) in all tRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_01037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH +
CC uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC methyluridine(54) in tRNA + NAD(+); Xref=Rhea:RHEA:16873, Rhea:RHEA-
CC COMP:10167, Rhea:RHEA-COMP:10193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57453, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.74;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH +
CC uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC methyluridine(54) in tRNA + NADP(+); Xref=Rhea:RHEA:62372, Rhea:RHEA-
CC COMP:10167, Rhea:RHEA-COMP:10193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.74;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01037};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01037};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01037}.
CC -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01037}.
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DR EMBL; AE007317; AAK99648.1; -; Genomic_DNA.
DR PIR; D97977; D97977.
DR RefSeq; NP_358438.1; NC_003098.1.
DR RefSeq; WP_000083698.1; NC_003098.1.
DR AlphaFoldDB; Q8DQ51; -.
DR SMR; Q8DQ51; -.
DR STRING; 171101.spr0844; -.
DR EnsemblBacteria; AAK99648; AAK99648; spr0844.
DR GeneID; 60233719; -.
DR GeneID; 66806070; -.
DR KEGG; spr:spr0844; -.
DR PATRIC; fig|171101.6.peg.932; -.
DR eggNOG; COG1206; Bacteria.
DR HOGENOM; CLU_033057_1_0_9; -.
DR OMA; MHRNTFL; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030698; F:5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_01037; TrmFO; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR040131; MnmG_N.
DR InterPro; IPR004417; TrmFO.
DR PANTHER; PTHR11806; PTHR11806; 1.
DR PANTHER; PTHR11806:SF2; PTHR11806:SF2; 1.
DR Pfam; PF01134; GIDA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00137; gid_trmFO; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Methyltransferase; NAD; NADP;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..444
FT /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT methyltransferase TrmFO"
FT /id="PRO_0000117273"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
SQ SEQUENCE 444 AA; 49287 MW; 0FA295DCD8BC3946 CRC64;
MSQSYINVIG AGLAGSEAAY QIAERGIPVK LYEMRGVKST PQHKTDNFAE LVCSNSLRGD
ALTNAVGLLK EEMRRLGSVI LESAEATRVP AGGALAVDRD GFSQMVTEKV ANHPLIEVVR
DEITELPTDV ITVIATGPLT SDALAEKIHA LNDGDGFYFY DAAAPIIDVN TIDMSKVYLK
SRYDKGEAAY LNAPMTKQEF MDFHEALVNA EEAPLNSFEK EKYFEGCMPI EVMAKRGIKT
MLYGPMKPVG LEYPDDYTGP RDGEFKTPYA VVQLRQDNAA GSLYNIVGFQ THLKWGEQKR
VFQMIPGLEN AEFVRYGVMH RNSYMDSPNL LEQTYRSKKQ PNLFFAGQMT GVEGYVESAA
SGLVAGINAA RLFKEESEVI FPETTAIGSL AHYITHADSK HFQPMNVNFG IIKELEGERI
RDKKARYEKI AERALADLEE FLTV
