ID   TRMFO_LAWIP             Reviewed;         445 AA.
AC   Q1MQ25;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=LI0848;
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the
RT   causative agent of proliferative enteropathy.";
RL   Submitted (NOV-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; AM180252; CAJ54902.1; -; Genomic_DNA.
DR   RefSeq; YP_595223.1; -.
DR   GeneID; 4060322; -.
DR   GenomeReviews; AM180252_GR; LI0848.
DR   KEGG; lip:LI0848; -.
DR   HOGENOM; Q1MQ25; -.
DR   OMA; Q1MQ25; MKPVGLT.
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    445       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase trmFO.
FT                                /FTId=PRO_0000346349.
FT   NP_BIND      10     15       FAD (By similarity).
SQ   SEQUENCE   445 AA;  49746 MW;  AF1D0E005E6956A3 CRC64;
     MNIHNIAIIG GGLSGCECAL TLAKFGFSVT LFEQKPQLFS PAHNTPLLAE LVCSNSLRSN
     ELTTGIGLLK QELRELNSPL MAIADTCRVP AGKALAVDRE LFSKQVTQLI ESHPKIHLIR
     EEVSSLSTSF LEKYDRIIVA TGPLASPNIS NSLSTLIGDK YLYFYDAIAP IVTADSIDMS
     IAFWGSRYEE QGEGDYLNCP MSYEEYQIFY SSLLKGEKVT NSKVEKEIHF EGCMPIEALA
     ERGEKTLLFG PFKPVGLINP HTGLRPYAVL QLRPENLNKS MLNLVGCQTK LTYPAQDTIF
     RLVPGLSNVE FVRFGSMHRN TYINSPKILT DQLALRNFPC IHLAGQITGV EGYVESIACG
     LWVSILLLAL SKDKKILRPP KTCALGGLLE HISCPSKQFQ PSNIHFGLVP EPTEKIKKKE
     RKEWYAQRAR IDFYHWLNNE LIHIM
//