NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

Comments

FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs (By similarity).
CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH₂ = tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD.
COFACTOR: FAD (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the mnmG family. TrmFO subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000040; BAC49992.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_771367.1; -.

3D structure databases

ModBase

Q89L21.

Enzyme and pathway databases

BioCyc

BJAP224911:BLR4727-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from HAMAP).
GO:0047151;	Molecular function: methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity (inferred from electronic annotation from EC).
GO:0016491;	Molecular function: oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0009021;	Molecular function: tRNA (uracil-5-)-methyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0008033;	Biological process: tRNA processing (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01037; -; 1.
PBIL [Tree]

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR004417; Gid.
IPR002218; GIDA.
IPR001100; Pyr_nuc-diS_OxRdtase.
Graphical view of domain structure.

PANTHER

PTHR11806; GIDA; 1.

Pfam

PF01134; GIDA; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.

ProDom

PD003738; GIDA; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00137; gid_trmFO; 1.

PROSITE

PS01280; GIDA_1; FALSE_NEG.
PS01281; GIDA_2; 1.

Genome annotation databases

GeneID

1052322; -.

GenomeReviews

BA000040_GR; blr4727.

KEGG

bja:blr4727; -.

NMPDR

fig|224911.1.peg.4727; -.

Phylogenomic databases

HOGENOM

Q89L21; -.

Genome annotation databases

CMR

Q89L21; blr4727.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase; Transferase; tRNA processing.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 475`	`475`	`Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase trmFO.`	`PRO_0000117237`
`NP_BIND`	`13 18`	`6`	`FAD (By similarity).`

Sequence information

Length: 475 AA [This is the length of the unprocessed precursor]

Molecular weight: 50908 Da [This is the MW of the unprocessed precursor]

CRC64: 7DE46881B1D39969 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTGPHSNIVH VIGAGLAGSE AAWQVAKAGV PVMLHEMRPD RMTEAHRTDG LAELVCSNSF 

        70         80         90        100        110        120 
RSDDAANNAV GLLHAEMRRL GSLIMRAADA NQVPAGGALA VDRDGFSAAV TKALNDHPLI 

       130        140        150        160        170        180 
EIARGEIAGL PPADWGNVIV ATGPLTSAPL ADAIRELTDE NALAFFDAIA PIVHRESIDM 

       190        200        210        220        230        240 
SVAWFQSRYD KVGPGGNGAD YINCPMTKEQ YEGFVAALIA GEKTEFKEWE TNTPYFDGCL 

       250        260        270        280        290        300 
PIEVMAERGP ETLRHGPMKP VGLTNPHDPT TKAYAIVQLR QDNKLGTLYN IVGFQTKLKY 

       310        320        330        340        350        360 
GEQQRIFRTI PGLEKAEFAR LGGLHRNTFL NSPKLLDGQL RLRAQPRLRF AGQMTGCEGY 

       370        380        390        400        410        420 
VESASVGLIA GLYAAADARG ETLASPPATT ALGSLLGHIT GGHIETIEPG TRSFQPMNIN 

       430        440        450        460        470 
FGLFPPLASA PTKKPDGTRL RGNEKTVAKK QAMSALALAD LDRWIADHLR IAAAA

Q89L21 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools