ID   TMFO1_MYCCT             Reviewed;         438 AA.
AC   Q2SS13;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase trmFO 1;
DE            EC=2.1.1.74;
DE   AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase 1;
DE   AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase 1;
GN   Name=trmFO1; OrderedLocusNames=MCAP_0476;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC
OS   27343 / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C.,
RA   Nierman W.C.;
RL   Submitted (SEP-2005) 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; CP000123; ABC01640.1; -; Genomic_DNA.
DR   RefSeq; YP_424450.1; -.
DR   GeneID; 3828914; -.
DR   GenomeReviews; CP000123_GR; MCAP_0476.
DR   KEGG; mcp:MCAP_0476; -.
DR   TIGR; MCAP_0476; -.
DR   HOGENOM; Q2SS13; -.
DR   OMA; Q2SS13; HKNYYIN.
DR   BioCyc; MCAP340047:MCAP_0476-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; 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   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    438       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase trmFO 1.
FT                                /FTId=PRO_0000346362.
FT   NP_BIND       9     14       FAD (By similarity).
SQ   SEQUENCE   438 AA;  49833 MW;  B2D86B36DA32AFE9 CRC64;
     MNKKVKIIGA GLAGCEAAYF LANNDIQVEL YEVKTLIKNE VQKTNNFAEL VCSNTFRSQS
     LLNAAGILKA EMRRLNSLVI KIADSCKIDG DDALAVDRED FSKKLTDVIK NHPNITIIEQ
     NVSYIDDEND LTLIATGPLT TNELKEDIQR LIGKQKLFFM DASAPIITKD SIDFNKVYYS
     GRHKQGKYIC CPLNEQEFNK FVDDLVNAEQ VQLKEFEKSI FFKGCQPIEQ LAKTSKKLLL
     KGPMSPNNLL DQNNQQPYAV VQLRQDDAKD SLYNMVGFQT NLKWPEQKRV FQTIPGLEKA
     KIVRYGVMHK NYYINSPKIL NFKLQVIRKK NVFFAGQITG VEGYIESASS GIWAAINILA
     FINNKKIKPL PNTTILGALT NYITNSKIYS LKPMKCNLGI LEQENKYQSN DKFYSYNNSK
     NSLENYIEQL NKILRTNI
//