ID   TRMFO_ANADE             Reviewed;         450 AA.
AC   Q2ILE0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase trmFO;
DE            EC=2.1.1.74;
DE   AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase;
DE   AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase;
GN   Name=trmFO; OrderedLocusNames=Adeh_2697;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-
CC       uridine at position 54 (M-5-U54) in all tRNAs (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + tRNA
CC       containing uridine at position 54 + FADH(2) = tetrahydrofolate +
CC       tRNA containing ribothymidine at position 54 + FAD.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the mnmG family. TrmFO subfamily.
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DR   EMBL; CP000251; ABC82467.1; -; Genomic_DNA.
DR   RefSeq; YP_465904.1; -.
DR   GeneID; 3890293; -.
DR   GenomeReviews; CP000251_GR; Adeh_2697.
DR   KEGG; ade:Adeh_2697; -.
DR   HOGENOM; Q2ILE0; -.
DR   OMA; Q2ILE0; MKPVGLT.
DR   BioCyc; ADEH290397:ADEH_2697-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:HAMAP.
DR   GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-...; IEA:EC.
DR   GO; GO:0009021; F:tRNA (uracil-5-)-methyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:HAMAP.
DR   HAMAP; MF_01037; -; 1.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004417; Gid.
DR   InterPro; IPR002218; GIDA-rel.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11806; GIDA; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   ProDom; PD003738; GIDA; 1.
DR   TIGRFAMs; TIGR00137; gid_trmFO; 1.
DR   PROSITE; PS01280; GIDA_1; FALSE_NEG.
DR   PROSITE; PS01281; GIDA_2; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW   Transferase; tRNA processing.
FT   CHAIN         1    450       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase trmFO.
FT                                /FTId=PRO_0000346317.
FT   NP_BIND      10     15       FAD (By similarity).
SQ   SEQUENCE   450 AA;  48369 MW;  C5C2BE25A871FDDD CRC64;
     MGDTRVTVIG GGLAGSEAAW QLARAGVAVE LVEMKPERRS PAHVLPGLAE LVCSNSLRSD
     NPQNAVGLLH EELRRLGSLV LGCADATRVP AGDALAVDRE RFSEAVTARL SGHPGVRIVH
     REVEDLPPPP ALAVIATGPL TGDALAARLA EATGGRLHFY DAIAPIVAAE SIDRSIAYAR
     SRYGKGSGDD YLNLPLDEAQ YHAFVDALLQ GEKVPAHGFE EPRYFEGCLP IEVMAERGTE
     VLAHGPLKPV GLEDPRTGRW PHAVVQLRRE DVEGTAWNLV GFQTRLTWPE QRRIFRAFLP
     GLANAEFVRL GQIHRNTFVD APRVLAPDLS VRAAPHLFLA GQITGVEGYV ESAACGLMAA
     RAVLDRLAER AFRPPPAATA LGALHRHLTG EAHPPGYDYQ PSNVVFALFP PLTGRHRGKA
     GRKEAHVERA RKELAPWIDT APPPAVPAAG
//