ID   TRMFO_HYPNA             Reviewed;         467 AA.
AC   Q0BYJ6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=HNE_2768;
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
RA   Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
RA   Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
RA   Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
RA   Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
RA   Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(2006).
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 + tRNA
CC       containing uridine at position 54 + FADH(2) = tetrahydrofolate +
CC       tRNA containing ribothymidine at position 54 + 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; CP000158; ABI75802.1; -; Genomic_DNA.
DR   RefSeq; YP_761447.1; -.
DR   GeneID; 4287632; -.
DR   GenomeReviews; CP000158_GR; HNE_2768.
DR   KEGG; hne:HNE_2768; -.
DR   NMPDR; fig|228405.5.peg.2654; -.
DR   TIGR; HNE_2768; -.
DR   HOGENOM; Q0BYJ6; -.
DR   OMA; Q0BYJ6; MKPVGLT.
DR   BioCyc; HNEP81032:HNE_2768-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:HAMAP.
DR   GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-...; IEA:EC.
DR   GO; GO:0009021; F:tRNA (uracil-5-)-methyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:HAMAP.
DR   HAMAP; MF_01037; -; 1.
DR   InterPro; IPR004417; Gid.
DR   InterPro; IPR002218; GIDA-rel.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11806; GIDA; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   ProDom; PD003738; 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    467       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase trmFO.
FT                                /FTId=PRO_0000346344.
FT   NP_BIND      10     15       FAD (By similarity).
SQ   SEQUENCE   467 AA;  50980 MW;  943568A29D5BC664 CRC64;
     MTLKPIHVIG GGMAGSEAAW QIASAGVPVI LHEMRGVRGT DAHQTDKLAE LVCSNSFRSD
     DHTTNAVGVI HEEMRRANGL IITTAKDHQV PAGSALAVDR EGFSEAITAK LEAHPLVTIV
     REEIAGLPPE DWDSVIVATG PLTSIALAEA VRAHTGETDL AFFDAIAPIV YFESIDMDKA
     WRQSRYDKAG PSGDTAAYIN CPMTEEQYNA FLDALLAAPK TEFRDWEKDT PYFEGCLPIE
     VMAERGRETL RFGPMKPVGL TNPHNPTVKA HAIVQLRQDN ALGTLWNMVG FQTKLKYAAQ
     TDIFRMIPGL EKAEFARLGG IHRNTFLNSP KLLDRQLRMK SMPRLRFAGQ VTGVEGYVES
     AAMGLLAGRF AAAERLGQRL EPPPPTTAMG ALISHITGGH LAEKQTFQPM NVNFGLFPDI
     TDYSKTDENG KRLRGKDKGR AKKIAQAIRA LQDFDAWLAG EAVVAAE
//