ID D3H8K0_STRM6 Unreviewed; 456 AA.
AC D3H8K0;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO {ECO:0000256|HAMAP-Rule:MF_01037};
DE EC=2.1.1.74 {ECO:0000256|HAMAP-Rule:MF_01037};
DE AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01037};
DE AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01037};
GN Name=gid {ECO:0000313|EMBL:CBJ22195.1};
GN Synonyms=trmFO {ECO:0000256|HAMAP-Rule:MF_01037};
GN OrderedLocusNames=smi_0948 {ECO:0000313|EMBL:CBJ22195.1};
OS Streptococcus mitis (strain B6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=365659 {ECO:0000313|EMBL:CBJ22195.1, ECO:0000313|Proteomes:UP000008563};
RN [1] {ECO:0000313|EMBL:CBJ22195.1, ECO:0000313|Proteomes:UP000008563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:CBJ22195.1,
RC ECO:0000313|Proteomes:UP000008563};
RX PubMed=20195536; DOI=10.1371/journal.pone.0009426;
RA Denapaite D., Brueckner R., Nuhn M., Reichmann P., Henrich B., Maurer P.,
RA Schaehle Y., Selbmann P., Zimmermann W., Wambutt R., Hakenbeck R.;
RT "The genome of Streptococcus mitis B6--what is a commensal?";
RL PLoS ONE 5:E9426-E9426(2010).
CC -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-uridine
CC at position 54 (M-5-U54) in all tRNAs. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01037};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_01037};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01037}.
CC -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01037}.
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DR EMBL; FN568063; CBJ22195.1; -; Genomic_DNA.
DR RefSeq; YP_003446060.1; NC_013853.1.
DR AlphaFoldDB; D3H8K0; -.
DR STRING; 365659.smi_0948; -.
DR KEGG; smb:smi_0948; -.
DR PATRIC; fig|365659.3.peg.949; -.
DR eggNOG; COG1206; Bacteria.
DR HOGENOM; CLU_033057_1_0_9; -.
DR OrthoDB; 9803114at2; -.
DR Proteomes; UP000008563; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047151; F:tRNA (uracil(54)-C5)-methyltransferase activity, 5,10-methylenetetrahydrofolate-dependent; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 NCBIfam; TIGR00137; gid_trmFO; 1.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF2; METHYLENETETRAHYDROFOLATE--TRNA-(URACIL-5-)-METHYLTRANSFERASE TRMFO; 1.
DR Pfam; PF01134; GIDA; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01037};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01037};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01037};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01037};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01037};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01037};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01037};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01037}.
FT DOMAIN 18..388
FT /note="MnmG N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01134"
FT BINDING 22..27
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01037"
SQ SEQUENCE 456 AA; 50430 MW; 5C58E9C0B237A27F CRC64;
MNLGSTQRGI SVVSQSYINV IGAGLAGSEA AYQIAERGIP VKLYEMRGVK STPQHKTDNF
AELVCSNSLR GDALTNAVGL LKEEMRRLGS VILKSAEATR VPAGGALAVD RDGFSQMVTE
KVTNHPLIEV VRDEITELPT DVITVVATGP LTSDALAEKI HALNDGDGFY FYDAAAPIID
VNTIDMSKVY LKSRYDKGEA AYLNAPMTKQ EFMDFHEALV NAEEAPLNSF EKEKYFEGCM
PIEVMAKRGI KTMLYGPMKP VGLEYPDDYT GPRDGEFKTP YAVVQLRQDN AAGSLYNIVG
FQTHLKWGEQ KRVFQMIPGL ENAEFVRYGV MHRNSYMDSP NLLEQTYRSK KQPNLFFAGQ
MTGVEGYVES AASGLVAGIN AARLFKGESE AIFPETTAIG SLAHYITHAD SKHFQPMNVN
FGIIKELEGE RIRDKKARYE KIAERALSDL EEFLTV
//
