ID   TMFO1_MESFL             Reviewed;         442 AA.
AC   Q6F1M4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   16-JUN-2009, entry version 44.
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=Mfl242;
OS   Mesoplasma florum (Acholeplasma florum).
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales;
OC   Entomoplasmataceae; Mesoplasma.
OX   NCBI_TaxID=2151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33453 / L1 / NBRC 100688 / NCTC 11704;
RA   Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA   Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R.,
RA   Nusbaum C.;
RL   Submitted (JUN-2004) 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; AE017263; AAT75599.1; -; Genomic_DNA.
DR   RefSeq; YP_053483.1; -.
DR   GeneID; 2897836; -.
DR   GenomeReviews; AE017263_GR; Mfl242.
DR   KEGG; mfl:Mfl242; -.
DR   HOGENOM; Q6F1M4; -.
DR   OMA; Q6F1M4; HKNYYIN.
DR   BioCyc; MFLO265311:MFL242-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; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW   Transferase; tRNA processing.
FT   CHAIN         1    442       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase trmFO 1.
FT                                /FTId=PRO_0000346354.
FT   NP_BIND       9     14       FAD (By similarity).
SQ   SEQUENCE   442 AA;  49761 MW;  C253B7257CAB22CB CRC64;
     MQKEVNIIGA GLAGCEAAYL LANNGVKVNL FEVKSLMKND IQKTNDLGEL VCSNTLRSKS
     KKNAAGILKN EMKLLNSLVI KAALENEIPG DDALSVDRFG FSKYITDKIK NHKNINLIEQ
     EVSEVDYTKV TIIASGPLTT DKLGKNIELM TGNEKLFFLD ASAPIITKDS IDFNKVYWAS
     RHNDGKDGQY ICIPLNEEQF NAFVEELKNA ETIKLKSFEK EIYFKGCQPI EQIAKTSKKV
     LLNGPLSPNN LIDENGNTPF AVVQLRQDDA IDSLYNFVGF QTNIKWPEQK RILQTLPGLE
     NLNIVRFGVM HKNYYINSPK LLNRSLQVKR NKNIFFAGQI TGVEGYIESA SSGILTAINV
     LAYLNNIKIE QPSRKSMLGA LNFYITNPKH DKLKPMKCNL GILDQQNKNA KSEFYSFDES
     EREIRRFIKG INNFAKIGEN NE
//