ID A0A1B8WJR0_9BACI Unreviewed; 439 AA.
AC A0A1B8WJR0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=trmFO {ECO:0000256|HAMAP-Rule:MF_01037};
GN ORFNames=A7975_02915 {ECO:0000313|EMBL:OBZ16870.1};
OS Bacillus sp. FJAT-26390.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743142 {ECO:0000313|EMBL:OBZ16870.1, ECO:0000313|Proteomes:UP000092623};
RN [1] {ECO:0000313|EMBL:OBZ16870.1, ECO:0000313|Proteomes:UP000092623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-26390 {ECO:0000313|EMBL:OBZ16870.1,
RC ECO:0000313|Proteomes:UP000092623};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Z., Chen Q., Liu B.,
RA Zhu Y., Wang J., Liu G.;
RT "Bacillus sp. FJAT-26390.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBZ16870.1}.
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DR EMBL; MAQX01000001; OBZ16870.1; -; Genomic_DNA.
DR RefSeq; WP_065384076.1; NZ_MAQX01000001.1.
DR AlphaFoldDB; A0A1B8WJR0; -.
DR Proteomes; UP000092623; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000092623};
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 6..369
FT /note="MnmG N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01134"
FT BINDING 11..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01037"
SQ SEQUENCE 439 AA; 48448 MW; 58EF566D0C52BB62 CRC64;
MSQPQKVTVI GAGLAGSEAA WQIASQGVPV VLYEMRPVTK TPAHHTNQFA ELVCSNSLRA
NGLTNAVGVL KEEMRQLNSL ILSCADQHAV PAGGALAVDR DGFSGEVTRR LHEHPLVEVR
NEEVTEIPTD GIVVIATGPL TAPGLSSQIQ ELLGEEYFYF YDAAAPIVEK DSIDMNKVYL
ASRYDKGEAA YLNCPMTEEE FEIFHEALTT AEKAEVKDFE KEVYFEGCMP IEVMASRGKQ
TVLFGPMKPV GLVNPHTGKL PHAVIQLRQD NAAGTLYNLV GFQTHLKWGE QKRVFSLIPG
LENAEFVRFG VMHRNTFINS PRLLKPTYQL NNRDTLFFAG QMTGVEGYVE SAASGLIAGI
NAAKLARGLE PVVLPEQTTL GSMANYITTA DFKHFQPMNA NFGLFPPLEK KIRSKKEKNE
MIANRALEGI EQFKREHLQ
//
