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P0A8I5 (TRMB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanine-N(7)-)-methyltransferase

EC=2.1.1.33
Alternative name(s):
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
Name:trmB
Synonyms:trmI, yggH
Ordered Locus Names:b2960, JW2927
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. HAMAP-Rule MF_01057

Catalytic activity

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. Ref.4

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_01057

Subunit structure

Monomer. Ref.4

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.

Sequence caution

The sequence AAA72956.1 differs from that shown. Reason: Frameshift at position 29.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 239239tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000171326

Regions

Region150 – 1556Interaction with RNA Potential
Region217 – 2204Substrate binding By similarity

Sites

Active site1441 By similarity
Binding site691S-adenosyl-L-methionine By similarity
Binding site941S-adenosyl-L-methionine By similarity
Binding site1211S-adenosyl-L-methionine By similarity
Binding site1441S-adenosyl-L-methionine By similarity
Binding site1481Substrate By similarity
Binding site1801Substrate By similarity

Experimental info

Mutagenesis261R → A: Reduces catalytic activity over 10-fold. Ref.5
Mutagenesis1441D → A: Loss of activity. Ref.5
Mutagenesis1501R → A: Reduces catalytic activity about 3-fold. Ref.5
Mutagenesis1511H → A: Reduces catalytic activity over 10-fold. Ref.5
Mutagenesis1521N → A: No effect. Ref.5
Mutagenesis1541R → A: Loss of activity. Ref.5
Mutagenesis1551R → A: Loss of activity. Ref.5
Mutagenesis1801D → A: Reduces catalytic activity over 10-fold. Ref.5
Mutagenesis2171T → A: Reduces catalytic activity over 10-fold. Ref.5
Mutagenesis2201E → A: Reduces catalytic activity 10-fold. Ref.5

Secondary structure

.............................. 239
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A8I5 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: B4C8AF9A1EF85FEB

FASTA23927,307
        10         20         30         40         50         60 
MKNDVISPEF DENGRPLRRI RSFVRRQGRL TKGQEHALEN YWPVMGVEFS EDMLDFPALF 

        70         80         90        100        110        120 
GREAPVTLEI GFGMGASLVA MAKDRPEQDF LGIEVHSPGV GACLASAHEE GLSNLRVMCH 

       130        140        150        160        170        180 
DAVEVLHKMI PDNSLRMVQL FFPDPWHKAR HNKRRIVQVP FAELVKSKLQ LGGVFHMATD 

       190        200        210        220        230 
WEPYAEHMLE VMSSIDGYKN LSESNDYVPR PASRPVTKFE QRGHRLGHGV WDLMFERVK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Escherichia coli micA gene required for A/G-specific mismatch repair: identity of micA and mutY."
Tsai-Wu J.-J., Radicella J.P., Lu A.-L.
J. Bacteriol. 173:1902-1910(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The yggH gene of Escherichia coli encodes a tRNA (m7G46) methyltransferase."
De Bie L.G.S., Roovers M., Oudjama Y., Wattiez R., Tricot C., Stalon V., Droogmans L., Bujnicki J.M.
J. Bacteriol. 185:3238-3243(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBUNIT.
Strain: K12 / XL1-Blue.
[5]"Sequence-structure-function relationships of a tRNA (m7G46) methyltransferase studied by homology modeling and site-directed mutagenesis."
Purta E., van Vliet F., Tricot C., De Bie L.G., Feder M., Skowronek K., Droogmans L., Bujnicki J.M.
Proteins 59:482-488(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-26; ASP-144; ARG-150; HIS-151; ASN-152; ARG-154; ARG-155; ASP-180; THR-217 AND GLU-220.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59471 Genomic DNA. Translation: AAA72956.1. Frameshift.
U28377 Genomic DNA. Translation: AAA69127.1.
U00096 Genomic DNA. Translation: AAC75997.1.
AP009048 Genomic DNA. Translation: BAE77023.1.
PIRG65081.
RefSeqNP_417435.1. NC_000913.3.
YP_491159.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DXXX-ray2.05A33-239[»]
3DXYX-ray1.50A33-239[»]
3DXZX-ray1.58A33-239[»]
ProteinModelPortalP0A8I5.
SMRP0A8I5. Positions 36-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36015N.
IntActP0A8I5. 45 interactions.
STRING511145.b2960.

Proteomic databases

PaxDbP0A8I5.
PRIDEP0A8I5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75997; AAC75997; b2960.
BAE77023; BAE77023; BAE77023.
GeneID12933364.
947448.
KEGGecj:Y75_p2890.
eco:b2960.
PATRIC32121334. VBIEscCol129921_3055.

Organism-specific databases

EchoBASEEB1727.
EcoGeneEG11779. trmI.

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000073968.
KOK03439.
OMAHSTLEMA.
OrthoDBEOG6K6VBC.
PhylomeDBP0A8I5.

Enzyme and pathway databases

BioCycEcoCyc:EG11779-MONOMER.
ECOL316407:JW2927-MONOMER.
MetaCyc:EG11779-MONOMER.
UniPathwayUPA00989.

Gene expression databases

GenevestigatorP0A8I5.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_01057. tRNA_methyltr_TrmB.
InterProIPR029063. SAM-dependent_MTases-like.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A8I5.
PROP0A8I5.

Entry information

Entry nameTRMB_ECOLI
AccessionPrimary (citable) accession number: P0A8I5
Secondary accession number(s): P32049, P58089, Q2M9N3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: June 11, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene