ID   TRMFO_ERYLH             Reviewed;         455 AA.
AC   Q2NAC8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=ELI_06355;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravits S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H.,
RA   Friedman R., Venter J.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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000157; ABC63363.1; -; Genomic_DNA.
DR   RefSeq; YP_458160.1; -.
DR   GeneID; 3871190; -.
DR   GenomeReviews; CP000157_GR; ELI_06355.
DR   KEGG; eli:ELI_06355; -.
DR   NMPDR; fig|314225.3.peg.1785; -.
DR   OMA; Q2NAC8; MKPVGLT.
DR   BioCyc; ELIT314225:ELI_06355-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   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    455       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase trmFO.
FT                                /FTId=PRO_0000346338.
FT   NP_BIND       9     14       FAD (By similarity).
SQ   SEQUENCE   455 AA;  50302 MW;  17AC398D39DA5AC4 CRC64;
     MSHDVHIIGG GLAGSEAAWQ LARRGVKVRL SEMRGSGEMT HAHQTDGLAE LVCSNSFRSD
     DDTKNAVGLL HYEMRALDSL VMRAGEVAQV PAGSAMAVDR DVFSAEVQKT LEAHPNIEVV
     RERVDALPEA GLTIVSTGPL TAQSLAESIV KATGQERLAF FDAIAPIVHR DSIDMSKCWI
     QSRWNKRTEA SNEDGDYINC PMTKEQYLAF HQGLIDGEKT EFREWEKDTP YFDGCMPIEI
     MAARGVETLR YGPMKGVGLD NPYDTSEEHP QGRWPYAVVQ LRQDNKLGTL WNMVGFQTKL
     KYGAQVELFR TIPGLENAEF ARLGGLHRNT FLNSPMVLDR QLRLKGAEHI RFAGQVTGCE
     GYVESAAVGL MAGMMTAKEL AGDVWQGPPR TTALGALLSH ITGDAEAETY QPMNINFGLF
     PPLHEVKKKQ RKEAYTTRAK SDLGEWIAHE VRVSA
//