ID TRMFO_STRA5 Reviewed; 444 AA.
AC Q8DZX5;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 68.
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; Synonyms=gid; OrderedLocusNames=SAG0969;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R.,
RA Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S.,
RA Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M.,
RA Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D.,
RA Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G.,
RA Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an
RT emerging human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAM99853.1; -; Genomic_DNA.
DR RefSeq; NP_687981.1; NC_004116.1.
DR ProteinModelPortal; Q8DZX5; -.
DR STRING; 208435.SAG0969; -.
DR EnsemblBacteria; AAM99853; AAM99853; SAG0969.
DR GeneID; 1013773; -.
DR KEGG; sag:SAG0969; -.
DR PATRIC; 19628768; VBIStrAga72745_0975.
DR eggNOG; COG1206; -.
DR HOGENOM; HOG000252054; -.
DR KO; K04094; -.
DR OMA; RFAGQIT; -.
DR ProtClustDB; PRK05335; -.
DR BioCyc; SAGA208435:GHVY-970-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 InterPro; IPR020595; GIDA-rel_CS.
DR Pfam; PF01134; 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 1 444 Methylenetetrahydrofolate--tRNA-(uracil-
FT 5-)-methyltransferase TrmFO.
FT /FTId=PRO_0000117270.
FT NP_BIND 10 15 FAD (By similarity).
SQ SEQUENCE 444 AA; 49511 MW; CA438676C26001C4 CRC64;
MSQSYINVIG AGLAGSEAAY QIAKRGIPVK LYEMRGVKST PQHKTDNFAE LVCSNSFRGD
SLTNAVGLLK EEMRRLDSII MRNGEAHRVP AGGAMAVDRE GYSEAVTEEI HKHPLIEVIR
DEITDIPGDA ITVIATGPLT SDSLAAKIHE LNGGDGFYFY DAAAPIVDKN TIDINKVYLK
SRYDKGEAAY LNCPMTKEEF MAFHEALTTA EEAPLNSFEK EKYFEGCMPI EVMAKRGIKT
MLYGPMKPVG LEYPEDYKGP RDGEFKTPYA VVQLRQDNAA GSLYNIVGFQ THLKWGEQKR
VFQMIPGLEN AEFVRYGVMH RNSYMDSPNL LNQTFATRKN PNLFFAGQMT GVEGYVESAA
SGLVAGINAV RRFNGESEVV FPQTTAIGAL PHYITHTDSK HFQPMNVNFG IIKELEGPRI
RDKKERYEAI ATRALKDLEK FLNY
//