ID   TRMFO_ANAVT             Reviewed;         438 AA.
AC   Q3MA89;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=Ava_2482;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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 + 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; CP000117; ABA22097.1; -; Genomic_DNA.
DR   RefSeq; YP_322992.1; -.
DR   GeneID; 3682833; -.
DR   GenomeReviews; CP000117_GR; Ava_2482.
DR   KEGG; ava:Ava_2482; -.
DR   NMPDR; fig|240292.3.peg.1737; -.
DR   HOGENOM; Q3MA89; -.
DR   OMA; Q3MA89; MKPVGLT.
DR   BioCyc; AVAR240292:AVA_2482-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    438       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase trmFO.
FT                                /FTId=PRO_1000084282.
FT   NP_BIND      10     15       FAD (By similarity).
SQ   SEQUENCE   438 AA;  48219 MW;  2BE00125BED6D8EF CRC64;
     MDQQPIQVIG GGLAGTEAAW QIAQAGVPVI LHEMRPKRFS PAHHTEHLAE LVCSNSFGAM
     ASDRAAGLLH EELRQLGSVV IAKADEHAVP AGGALAVDRG QFGQDLTQTL ASHPLVEFRR
     SEVPAIPEGI VVLATGPLTS PDLAADLHRF TGMEYMSFFD AASPIIVGDS INRDIAFMAS
     RYDKGEAAYL NCPMNKEQYL RFREELCKAE QTELKDFERE TAKFFEACLP IEELAQRGED
     TMRYGPVKPV GLSDSRTGER PYAVVQLRQE DKAGQLWNMV GFQTNLRWGE QKRVFQMIPG
     LEKAEFVRLG VMHRNTFINA PQLMLPTLQF KQRPTLLAAG QLIGTEGYTA AAAGGWLAGT
     NAARLALGKE PLALPPTTML GALLEFISSA SPKHFQPMPP NFGILPDLGM KIKSKPERYG
     RYRDRSLADL SSWKHNLN
//