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 01-MAY-2013, entry version 56.
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 + 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; 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 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: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 1 446 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
//
