TRMFO_STRPQ
ID TRMFO_STRPQ Reviewed; 448 AA.
AC P0DB37; Q8K7G4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
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=SPs1022;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC64117.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000034; BAC64117.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_032461335.1; NC_004606.1.
DR AlphaFoldDB; P0DB37; -.
DR SMR; P0DB37; -.
DR KEGG; sps:SPs1022; -.
DR HOGENOM; CLU_033057_1_0_9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC.
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; Transferase;
KW tRNA processing.
FT CHAIN 1..448
FT /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT methyltransferase TrmFO"
FT /id="PRO_0000411356"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
SQ SEQUENCE 448 AA; 49448 MW; A7185DA471557AAA CRC64;
MSQSTATYIN VIGAGLAGSE AAYQIAKRGI PVKLYEMRGV KATPQHKTTN FAELVCSNSF
RGDSLTNAVG LLKEEMRRLD SIIMRNGEAN RVPAGGAMAV DREGYAKSVT AELENHPLIE
VIRDEITEIP NDAITVIATG PLTSDALAEK IHAVNGGDGF YFYDAAAPII DKSTIDMSKV
YLKSRYDKGE AAYLNCPMTK EEFMAFHEAL TTAEEAPLNS FEKEKYFEGC MPIEVMAKRG
IKTMLYGPMK PVGLEYPDDY TGPRDGEFKT PYAVVQLRQD NAAGSLYNIV GFQTHLKWGE
QKRVFQMIPG LENAEFVRYG VMHRNSYMDS PNLLTETFQS RSNPNLLFAG QMTGVEGYVE
SAASGLVAGI NAARLFKREE ALIFPQTTAI GSLPHYVTHA DSKHFQPMNV NFGIIKELEG
PRIRDKKERY EAIASRALAD LDTCLASL