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Database: UniProt
Entry: Q6MHW5
LinkDB: Q6MHW5
Original site: Q6MHW5 
ID   TRMFO_BDEBA             Reviewed;         440 AA.
AC   Q6MHW5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-APR-2014, entry version 73.
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=Bd3419;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529
OS   / HD100).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F.,
RA   Sockett R.E., Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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 + uracil(54) in
CC       tRNA + FADH(2) = tetrahydrofolate + 5-methyluracil(54) in tRNA +
CC       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; BX842655; CAE78217.1; -; Genomic_DNA.
DR   RefSeq; NP_970158.1; NC_005363.1.
DR   ProteinModelPortal; Q6MHW5; -.
DR   STRING; 264462.Bd3419; -.
DR   EnsemblBacteria; CAE78217; CAE78217; Bd3419.
DR   GeneID; 2737076; -.
DR   KEGG; bba:Bd3419; -.
DR   PATRIC; 21081146; VBIBdeBac73187_3128.
DR   eggNOG; COG1206; -.
DR   HOGENOM; HOG000252054; -.
DR   KO; K04094; -.
DR   OMA; RFAGQIT; -.
DR   OrthoDB; EOG6J74VT; -.
DR   ProtClustDB; PRK05335; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030698; F:5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.720; -; 2.
DR   HAMAP; MF_01037; TrmFO; 1.
DR   InterPro; IPR004417; Folate-dep_Ribothymidyl_synth.
DR   InterPro; IPR002218; GIDA-rel.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF01134; GIDA; 1.
DR   TIGRFAMs; TIGR00137; gid_trmFO; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW   Transferase; tRNA processing.
FT   CHAIN         1    440       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase TrmFO.
FT                                /FTId=PRO_0000346323.
FT   NP_BIND      14     19       FAD (By similarity).
SQ   SEQUENCE   440 AA;  49807 MW;  9D983B692AB975A7 CRC64;
     MTNITQNQKI TVVGAGLAGS ECALQLADMG YSVVLYEMRD KTMTPAHKTH KFAELVCSNS
     FGSLGEHSAP GQLKWEAKKL NSHILQAAFE AQVPAGQALG MDREVFSAIM TEKVKNHPNI
     EIRNDVVKSL NDIPRPAVIA TGPLTHDDLA ESMRQHFGDE FLYFFDAIAP IIDADSINTE
     IAWKADRYDK GTGDYYNCPM NKEEYNRFIE EIQKARKIEP KDFETTDFFE GCMPIEVMVD
     RGPQTLRFGP MKPIGLDDPR TGRYPWAVVQ LRQDNKEGTA YNMVGFQTRM AYGEQVRVFR
     MIPGLENAEF LKLGSIHRNL FINSPKRLNK DLSSKNDPWL FFAGQITGVE GYFESTCTGL
     MVSRFLNQKL KDQPFNPPPR ESAFGSLLEA ITDPTRAEHF QPTNINFALL PPLAEKERDK
     TLRKEKQIAI ARNVMEQWNP
//
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