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Database: UniProt
Entry: Q5NPP5
LinkDB: Q5NPP5
Original site: Q5NPP5 
ID   TRMFO_ZYMMO             Reviewed;         446 AA.
AC   Q5NPP5;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   19-FEB-2014, entry version 59.
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=ZMO0691;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J.,
RA   Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M.,
RA   Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y.,
RA   Kang H.L., Lee S.Y., Lee K.J., Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
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; AE008692; AAV89315.1; -; Genomic_DNA.
DR   RefSeq; YP_162426.1; NC_006526.2.
DR   ProteinModelPortal; Q5NPP5; -.
DR   STRING; 264203.ZMO0691; -.
DR   EnsemblBacteria; AAV89315; AAV89315; ZMO0691.
DR   GeneID; 3189439; -.
DR   KEGG; zmo:ZMO0691; -.
DR   PATRIC; 32566694; VBIZymMob102260_0655.
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   GO; GO:0030488; P:tRNA methylation; IEA:GOC.
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; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW   Transferase; tRNA processing.
FT   CHAIN         1    446       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase TrmFO.
FT                                /FTId=PRO_0000117285.
FT   NP_BIND       8     13       FAD (By similarity).
SQ   SEQUENCE   446 AA;  49770 MW;  3991C3FBEA9AEB69 CRC64;
     MQPVNIIGGG LAGSEAAWQL ASRQIPVRLF EMRGREKTPA HSTDKLAELV CSNSFRSDDP
     NSNAVGVLHA EMRKMGSLIM MIADQHRVPA GSALAVDREG FAEAVTNRLQ NHPLIEIHRE
     RIDHIPDETT IIASGPLTSD SLANAITELT GRDALSFFDA IAPIVYRDSI DMDIAWFQSR
     WDKGDGHDYI NCPLNKEEYL AFHAALLAGE KGDFHEWEKD TPYFEGCMPI EVMADRGIDT
     LRFGPMKPVG LDDPRTGRWP YGAVQLRQDN ALGTLWNMVG FQTKLKYAEQ IRIFRMIPGL
     EKAEFARLGG MHRNSFIRSP VLLDEYLRLK KQTNIRFAGQ ITGCEGYIES ASIGLLAGIF
     TAADKLDKKV SSPPVESALG ALLGHITKNA DPDHYQPMNI NFGLFPPISE KHPKKQRKAM
     MAERARKALD QWISEEAFLK SSILEQ
//
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