TRMFO_BACSU
ID TRMFO_BACSU Reviewed; 435 AA.
AC P39815; Q6LCY5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 148.
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, ECO:0000269|PubMed:16027442, ECO:0000269|PubMed:17673080};
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, ylyC;
GN OrderedLocusNames=BSU16130;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Foulger D., Errington J.;
RT "Cloning and sequencing 7.5 Kbp of DNA from Bacillus subtilis upstream of
RT the codV gene.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-363.
RC STRAIN=168 / 8G5;
RA de Jong S.;
RT "Cloning and sequencing of the TopI gene, the gene encoding B. subtilis DNA
RT topoisomerase I.";
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-435.
RC STRAIN=168 / JH642;
RX PubMed=7783641; DOI=10.1111/j.1365-2958.1995.tb02378.x;
RA Slack F.J., Serror P., Joyce E., Sonenshein A.L.;
RT "A gene required for nutritional repression of the Bacillus subtilis
RT dipeptide permease operon.";
RL Mol. Microbiol. 15:689-702(1995).
RN [5]
RP FUNCTION AS A TRNA(M-5-U54)-METHYLTRANSFERASE, CATALYTIC ACTIVITY,
RP COFACTOR, AND SUBUNIT.
RX PubMed=16027442; DOI=10.1093/nar/gki703;
RA Urbonavicius J., Skouloubris S., Myllykallio H., Grosjean H.;
RT "Identification of a novel gene encoding a flavin-dependent tRNA:m5U
RT methyltransferase in bacteria - evolutionary implications.";
RL Nucleic Acids Res. 33:3955-3964(2005).
RN [6]
RP FUNCTION AS A TRNA(M-5-U54)-METHYLTRANSFERASE, AND CATALYTIC ACTIVITY.
RX PubMed=17673080; DOI=10.1016/s0076-6879(07)25004-9;
RA Urbonavicius J., Brochier-Armanet C., Skouloubris S., Myllykallio H.,
RA Grosjean H.;
RT "In vitro detection of the enzymatic activity of folate-dependent tRNA
RT (Uracil-54,-C5)-methyltransferase: evolutionary implications.";
RL Methods Enzymol. 425:103-119(2007).
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, ECO:0000269|PubMed:16027442,
CC ECO:0000269|PubMed:17673080}.
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 ECO:0000269|PubMed:16027442, ECO:0000269|PubMed:17673080};
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 ECO:0000269|PubMed:16027442, ECO:0000269|PubMed:17673080};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01037,
CC ECO:0000305|PubMed:16027442};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:16027442}.
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, ECO:0000305}.
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DR EMBL; AJ000975; CAA04423.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13486.1; -; Genomic_DNA.
DR EMBL; L27797; AAA22764.1; -; Genomic_DNA.
DR EMBL; U13634; AAB03368.1; -; Genomic_DNA.
DR PIR; A69632; A69632.
DR RefSeq; NP_389495.1; NC_000964.3.
DR RefSeq; WP_003244725.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P39815; -.
DR SMR; P39815; -.
DR STRING; 224308.BSU16130; -.
DR jPOST; P39815; -.
DR PaxDb; P39815; -.
DR PRIDE; P39815; -.
DR DNASU; 938816; -.
DR EnsemblBacteria; CAB13486; CAB13486; BSU_16130.
DR GeneID; 938816; -.
DR KEGG; bsu:BSU16130; -.
DR PATRIC; fig|224308.179.peg.1753; -.
DR eggNOG; COG1206; Bacteria.
DR InParanoid; P39815; -.
DR OMA; MHRNTFL; -.
DR PhylomeDB; P39815; -.
DR BioCyc; BSUB:BSU16130-MON; -.
DR BRENDA; 2.1.1.74; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
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 Cytoplasm; FAD; Flavoprotein; Methyltransferase; NAD; NADP;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..435
FT /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT methyltransferase TrmFO"
FT /id="PRO_0000117234"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
SQ SEQUENCE 435 AA; 48063 MW; 6C7AB028F484B683 CRC64;
MNQQTVNVIG AGLAGSEAAW QLAKRGIQVK LYEMRPVKQT PAHHTDKFAE LVCSNSLRSN
TLANAVGVLK EEMRALDSAI IAAADECSVP AGGALAVDRH EFAASVTNRV KNHPNVTVIN
EEVTEIPEGP TIIATGPLTS ESLSAQLKEL TGEDYLYFYD AAAPIVEKDS LDMDKVYLKS
RYDKGEAAYL NCPMTEEEFD RFHEALTSAE TVPLKEFEKE IFFEGCMPIE VMAKRGKKTM
LFGPMKPVGL EHPVTGKRPY AVVQLRQDDA AGTLYNIVGF QTHLKWGDQK EVLKLIPGLE
NVEIVRYGVM HRNTFINSPS LLKPTYQFKN RSDLFFAGQM TGVEGYVESA ASGLVAGINA
AKLVLGEELV IFPQETAIGS MAHYITTTNQ KNFQPMNANF GLLKELPVKI KNKKERNEQY
ANRAIETIQT ISKTI
