ID TRMFO_GEOUR Reviewed; 435 AA.
AC A5G7S3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 46.
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=Gura_3688;
OS Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=351605;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rf4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Shelobolina E., Aklujkar M., Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-2007) 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 + uridine(54)
CC in tRNA + FADH(2) = tetrahydrofolate + 5-methyluridine(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; CP000698; ABQ27841.1; -; Genomic_DNA.
DR RefSeq; YP_001232414.1; NC_009483.1.
DR ProteinModelPortal; A5G7S3; -.
DR STRING; 351605.Gura_3688; -.
DR EnsemblBacteria; ABQ27841; ABQ27841; Gura_3688.
DR GeneID; 5165810; -.
DR KEGG; gur:Gura_3688; -.
DR PATRIC; 22037788; VBIGeoUra13052_3943.
DR eggNOG; COG1206; -.
DR HOGENOM; HOG000252054; -.
DR KO; K04094; -.
DR OMA; RFAGQIT; -.
DR ProtClustDB; PRK05335; -.
DR BioCyc; GURA351605:GI6A-3745-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030698; F:5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity; IEA:HAMAP.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:HAMAP.
DR GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:EC.
DR HAMAP; MF_01037; TrmFO; 1; -.
DR InterPro; IPR004417; Folate-dep_Ribothymidyl_synth.
DR InterPro; IPR002218; GIDA-rel.
DR Pfam; PF01134; 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 1 435 Methylenetetrahydrofolate--tRNA-(uracil-
FT 5-)-methyltransferase TrmFO.
FT /FTId=PRO_0000346341.
FT NP_BIND 10 15 FAD (By similarity).
SQ SEQUENCE 435 AA; 46993 MW; 071C10F2341B4083 CRC64;
MIKEKLTIIG AGLAGCEAAW QAAGRGVAVT LHEMKPEKYS PAHHLPGLAE LVCSNSLRGE
SLENAVGLLK EELRRLGSLF MEAALATRVP AGGALAVDRG LFSAFITDKI ENHPLIEVVH
GEVAEIPADG TVIVASGPLT SDALAASIGK YTGDYLYFYD AIAPIVTSDS IDLSKAFRAS
RYGKGDGDDY LNCPLDEAEY KAFIAALLAA EKVAAKEFEK VVHFEGCMPI EEMAERGLDT
LRFGPMKPVG LIDPRTGIEP HAVVQLRQEN REGTLFNLVG FQTKLTYPEQ QRIFRTIPGL
GKAEFVRLGS MHRNTFINAP QLLLSTFQLK REPRILFAGQ ITGVEGYVES AASGFLAGLN
GARLAKGEAL IVPPSVTALG ALVNHITSAP AKHFQPMNIN YGLFPDLAGR VKKKEKRAKL
AERALTELDG WMNTL
//
