TRMFO_THET8
ID TRMFO_THET8 Reviewed; 443 AA.
AC Q5SID2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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}; OrderedLocusNames=TTHA1442;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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: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; AP008226; BAD71265.1; -; Genomic_DNA.
DR RefSeq; WP_011228685.1; NC_006461.1.
DR RefSeq; YP_144708.1; NC_006461.1.
DR PDB; 3G5Q; X-ray; 2.10 A; A=1-443.
DR PDB; 3G5R; X-ray; 1.60 A; A=1-443.
DR PDB; 3G5S; X-ray; 1.05 A; A=1-443.
DR PDBsum; 3G5Q; -.
DR PDBsum; 3G5R; -.
DR PDBsum; 3G5S; -.
DR AlphaFoldDB; Q5SID2; -.
DR SMR; Q5SID2; -.
DR STRING; 300852.55772824; -.
DR PRIDE; Q5SID2; -.
DR EnsemblBacteria; BAD71265; BAD71265; BAD71265.
DR GeneID; 3169920; -.
DR KEGG; ttj:TTHA1442; -.
DR PATRIC; fig|300852.9.peg.1416; -.
DR eggNOG; COG1206; Bacteria.
DR HOGENOM; CLU_033057_1_0_0; -.
DR OMA; MHRNTFL; -.
DR PhylomeDB; Q5SID2; -.
DR BRENDA; 2.1.1.74; 2305.
DR EvolutionaryTrace; Q5SID2; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Methyltransferase; NAD; NADP;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..443
FT /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT methyltransferase TrmFO"
FT /id="PRO_0000346420"
FT BINDING 8..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3G5S"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:3G5S"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3G5S"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 343..361
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 374..384
FT /evidence="ECO:0007829|PDB:3G5S"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:3G5S"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:3G5Q"
FT HELIX 409..429
FT /evidence="ECO:0007829|PDB:3G5S"
SQ SEQUENCE 443 AA; 48863 MW; C3D2B7B800C4A107 CRC64;
MERVNVVGAG LAGSEAAWTL LRLGVPVRLF EMRPKRMTPA HGTDRFAEIV CSNSLGGEGE
TNAKGLLQAE MRRAGSLVME AADLARVPAG GALAVDREEF SGYITERLTG HPLLEVVREE
VREIPPGITV LATGPLTSEA LAEALKRRFG DHFLAYYDAA SPIVLYESID LTKCFRAGRY
GQSADYLNCP MTEEEYRRFH QALLEAQRHT PHDWEKLEFF EACVPVEELA RRGYQTLLFG
PMKPVGLVDP RTGKEPFAVV QLRQEDKAGR MWSLVGFQTG LKWPEQKRLI QMIPGLENAE
IVRYGVMHRN TYLNAPRLLG ETLEFREAEG LYAAGVLAGV EGYLESAATG FLAGLNAARK
ALGLPPVAPP EESMLGGLVR YLATANPEGF QPMYANWGLV PPVEGRMGKK EKRQAMYRRG
LEAFSAWLSG LNPPLPRPEA ALV
