TRMFO_STRMU
ID TRMFO_STRMU Reviewed; 444 AA.
AC P05428; Q9R306; Q9R7U1;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=SMU_1003;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-444.
RC STRAIN=MT4239 / Serotype c, MT4245 / Serotype e, MT4251 / Serotype f,
RC MT4467 / Serotype e, and MT8148 / Serotype c;
RX PubMed=9570124; DOI=10.1111/j.1574-6968.1998.tb12965.x;
RA Fujiwara T., Terao Y., Hoshino T., Kawabata S., Ooshima T., Sobue S.,
RA Kimura S., Hamada S.;
RT "Molecular analyses of glucosyltransferase genes among strains of
RT Streptococcus mutans.";
RL FEMS Microbiol. Lett. 161:331-336(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 359-444.
RC STRAIN=GS-5;
RX PubMed=3040685; DOI=10.1128/jb.169.9.4263-4270.1987;
RA Shiroza T., Ueda S., Kuramitsu H.K.;
RT "Sequence analysis of the gtfB gene from Streptococcus mutans.";
RL J. Bacteriol. 169:4263-4270(1987).
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; AE014133; AAN58704.1; -; Genomic_DNA.
DR EMBL; D88651; BAA26100.1; -; Genomic_DNA.
DR EMBL; D88654; BAA26104.1; -; Genomic_DNA.
DR EMBL; D88657; BAA26108.1; -; Genomic_DNA.
DR EMBL; D88660; BAA26112.1; -; Genomic_DNA.
DR EMBL; D89977; BAA26118.1; -; Genomic_DNA.
DR EMBL; M17361; AAA88587.1; -; Genomic_DNA.
DR PIR; A33135; A33135.
DR RefSeq; NP_721398.1; NC_004350.2.
DR RefSeq; WP_002262867.1; NC_004350.2.
DR AlphaFoldDB; P05428; -.
DR SMR; P05428; -.
DR STRING; 210007.SMU_1003; -.
DR PRIDE; P05428; -.
DR EnsemblBacteria; AAN58704; AAN58704; SMU_1003.
DR GeneID; 66817581; -.
DR KEGG; smu:SMU_1003; -.
DR PATRIC; fig|210007.7.peg.896; -.
DR eggNOG; COG1206; Bacteria.
DR HOGENOM; CLU_033057_1_0_9; -.
DR OMA; MHRNTFL; -.
DR PhylomeDB; P05428; -.
DR Proteomes; UP000002512; Chromosome.
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;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..444
FT /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT methyltransferase TrmFO"
FT /id="PRO_0000117271"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
FT VARIANT 255
FT /note="Q -> H (in strain: MT4239)"
SQ SEQUENCE 444 AA; 49552 MW; EA419B193C842695 CRC64;
MSQSYINVVG AGLAGSEAAY QIAKRGIPVK LYEMRGVKRT PQHKTSNFAE LVCSNSFRGD
SLTNAVGLLK EEMRRLDSII MRTGEAHRVP AGGAMAVDRS GYAQAVTAEL ENNPLIQVIR
NEVTEIPDDA ITVIATGPLT SDSLAKKIYK LNGGEGFYFY DAAAPIVDQS SIDMDKVYLK
SRYDKGEAAY LNCPMTKEEF IRFYEALINA EEAPFNSFER EKYFEGCMPI EVMAKRGIKT
LLYGPMKPVG LEYPQDYKGP RDGDYKAPYA VVQLRQDNAA GSLYNIVGFQ THLKWSEQKR
VFSMIPGLEQ AHFVRYGVMH RNSYIDSPNL LAPTFATCKN PNLFFAGQMT GVEGYVESAA
SGLVAGINAV RRFKDEEAVI FPQTTAIGAL PYYITHTKSK HFQPMNINFG IIKDLGGPRI
RDKKKRYEKI AERSLKDLQQ FLTV
