ID TRMFO_GEOSM Reviewed; 435 AA.
AC C6E557;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 01-MAY-2013, 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=GM21_1530;
OS Geobacter sp. (strain M21).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) 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; CP001661; ACT17586.1; -; Genomic_DNA.
DR RefSeq; YP_003021344.1; NC_012918.1.
DR ProteinModelPortal; C6E557; -.
DR STRING; 443144.GM21_1530; -.
DR EnsemblBacteria; ACT17586; ACT17586; GM21_1530.
DR GeneID; 8136859; -.
DR KEGG; gem:GM21_1530; -.
DR PATRIC; 22017506; VBIGeoSp56140_1487.
DR eggNOG; COG1206; -.
DR HOGENOM; HOG000252054; -.
DR KO; K04094; -.
DR OMA; RFAGQIT; -.
DR ProtClustDB; PRK05335; -.
DR BioCyc; GSP443144:GHKM-1560-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_1000213383.
FT NP_BIND 9 14 FAD (By similarity).
SQ SEQUENCE 435 AA; 47749 MW; 1DC9DF29DEFE9969 CRC64;
MTQQITVIGG GLAGCEAAWQ AAKRGVKVRL FEMKPNCYSE AHHLPGLSEL VCSNSLRGDS
LENAVGLLKE ELRRLESLFM EGAEATKVPA GGALAVDRDL FSQYITSRIE SHPLIEVVRE
EVTRIPEEGI VVLASGPLTA GLLAQEIGRL AGSYLYFYDA IAPIVAADSI DYGKAFRASR
YGKGDGDDYV NCPMDEEQYQ AFVREILAAE KVEPKSFEKV VHFEGCMPIE EMASRGPETL
RFGPMKPVGL VDPRVGVEPH AVIQLRQENL EATMYNLVGF QTKLTWPEQK RIFRMIPGLE
NAQFLRLGSM HRNTFINAPE LLMATCQLKS DQRIFFAGQI TGVEGYVESA SSGFAVGVNA
ARLSKGEGLV VPPAETAIGA LARHITNTEA AHFQPMNVNY GLFPPLPGRI KKKEKRGLLA
QRGLEALEMW LPELS
//
