TRMFO_MYXXD
ID TRMFO_MYXXD Reviewed; 457 AA.
AC Q9S449; Q1D807; Q84F98;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, 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, gidA;
GN OrderedLocusNames=MXAN_3007;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10844655; DOI=10.1046/j.1365-2958.2000.01887.x;
RA White D.J., Hartzell P.L.;
RT "AglU, a protein required for gliding motility and spore maturation in
RT Myxococcus xanthus, is related to WD-repeat proteins.";
RL Mol. Microbiol. 36:662-678(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12828649; DOI=10.1046/j.1365-2958.2003.03582.x;
RA Youderian P.A., Burke N., White D.J., Hartzell P.L.;
RT "Identification of genes required for adventurous gliding motility in
RT Myxococcus xanthus with the transposable element mariner.";
RL Mol. Microbiol. 49:555-570(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN [4]
RP FAD-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11703671; DOI=10.1046/j.1365-2958.2001.02659.x;
RA White D.J., Merod R., Thomasson B., Hartzell P.L.;
RT "GidA is an FAD-binding protein involved in development of Myxococcus
RT xanthus.";
RL Mol. Microbiol. 42:503-517(2001).
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 ECO:0000269|PubMed:11703671};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01037,
CC ECO:0000269|PubMed:11703671}.
CC -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01037}.
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DR EMBL; AF162663; AAD46374.1; -; Genomic_DNA.
DR EMBL; AY204472; AAO22919.1; -; Genomic_DNA.
DR EMBL; CP000113; ABF92331.1; -; Genomic_DNA.
DR RefSeq; WP_011553063.1; NC_008095.1.
DR AlphaFoldDB; Q9S449; -.
DR SMR; Q9S449; -.
DR STRING; 246197.MXAN_3007; -.
DR EnsemblBacteria; ABF92331; ABF92331; MXAN_3007.
DR GeneID; 41360368; -.
DR KEGG; mxa:MXAN_3007; -.
DR eggNOG; COG1206; Bacteria.
DR HOGENOM; CLU_033057_1_0_7; -.
DR OMA; MHRNTFL; -.
DR OrthoDB; 516534at2; -.
DR Proteomes; UP000002402; 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; 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.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; Methyltransferase; NAD; NADP;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..457
FT /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT methyltransferase TrmFO"
FT /id="PRO_0000117253"
FT BINDING 12..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
FT CONFLICT 126..127
FT /note="EQ -> DE (in Ref. 1; AAD46374)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="Y -> S (in Ref. 1; AAD46374)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="D -> N (in Ref. 1; AAD46374)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="Q -> H (in Ref. 1; AAD46374)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="R -> L (in Ref. 1; AAD46374)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="I -> M (in Ref. 1; AAD46374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 49764 MW; BE51C4E247353970 CRC64;
MADQKQRVTV IGGGLAGTEC AYQLSRRGVP VVLREMKPQK RSPAHKSDTL AELVCSNSLR
SDNPESAIGL LHAELRALGS LVLSAADANR VPAGDALAVE RERFSAAITE SLLRQPGVEL
VAGEVEQLPE DGPVVIATGP LTSDALTREL ERHVGTRLYF YDSIAPILSA DSIDMNVAFR
QSRYGKGGGD DYLNLPMTKD EYYRFIAEVK AGQKVVPHAF EEPKYFEGCL PIEVMAERGD
DTLAYGPMKP VGLRDPRTGQ EPYAVVQLRM EDVGGTSWNM VGFQTRLTWG EQKRIFSSFI
PGLQQAEFLR MGQIHRNTFI DSPRLLAKDL SLKTEPRLYF AGQISGVEGY VESAACGYLV
ALALHARLTG TEFVPPPATT AMGALLRHVT GEAHPPDYPH QPSNISFGIF SPLTGRMKKA
EKRAAYSARA KQDLAAWLPH AGVPAAGAPE HVDQRSA