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B1LJF4 (TGT_ECOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Queuine tRNA-ribosyltransferase

EC=2.4.2.29
Alternative name(s):
Guanine insertion enzyme
tRNA-guanine transglycosylase
Gene names
Name:tgt
Ordered Locus Names:EcSMS35_0438
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) By similarity. HAMAP-Rule MF_00168

Catalytic activity

Guanine34 in tRNA + queuine = queuosine34 in tRNA + guanine. HAMAP-Rule MF_00168

Guanine34 in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine34 in tRNA + guanine. HAMAP-Rule MF_00168

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00168

Pathway

tRNA modification; tRNA-queuosine biosynthesis. HAMAP-Rule MF_00168

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Ontologies

Keywords
   Biological processQueuosine biosynthesis
tRNA processing
   LigandMetal-binding
Zinc
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processqueuosine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

queuine tRNA-ribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Queuine tRNA-ribosyltransferase HAMAP-Rule MF_00168
PRO_1000198001

Sites

Active site891Nucleophile By similarity
Metal binding3021Zinc By similarity
Metal binding3041Zinc By similarity
Metal binding3071Zinc By similarity
Metal binding3331Zinc By similarity
Binding site901Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B1LJF4 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 40271CA08D8A8820

FASTA37542,594
        10         20         30         40         50         60 
MKFELDTTDG RARRGRLVFD RGVVETPCFM PVGTYGTVKG MTPEEVEATG AQIILGNTFH 

        70         80         90        100        110        120 
LWLRPGQEIM KLHGDLHDFM QWKGPILTDS GGFQVFSLGD IRKITEQGVH FRNPINGDPI 

       130        140        150        160        170        180 
FLDPEKSMEI QYDLGSDIVM IFDECTPYPA DWDYAKRSME MSLRWAKRSR ERFDSLGNKN 

       190        200        210        220        230        240 
ALFGIIQGSV YEDLRDISVK GLVDIGFDGY AVGGLAVGEP KADMHRILEH VCPQIPADKP 

       250        260        270        280        290        300 
RYLMGVGKPE DLVEGVRRGI DMFDCVMPTR NARNGHLFVT DGVVKIRNAK YKSDTGPLDP 

       310        320        330        340        350        360 
ECDCYTCRNY SRAYLHHLDR CNEILGARLN TIHNLRYYQR LMAGLRKAIE EGKLESFVTD 

       370 
FYQRQGREVP PLNVD 

« Hide

References

[1]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SMS-3-5 / SECEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000970 Genomic DNA. Translation: ACB16174.1.
RefSeqYP_001742541.1. NC_010498.1.

3D structure databases

ProteinModelPortalB1LJF4.
SMRB1LJF4. Positions 3-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439855.EcSMS35_0438.

Proteomic databases

PRIDEB1LJF4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB16174; ACB16174; EcSMS35_0438.
GeneID6146420.
KEGGecm:EcSMS35_0438.
PATRIC18429719. VBIEscCol6161_0611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0343.
HOGENOMHOG000223473.
KOK00773.
OMAFGSDIIM.
OrthoDBEOG6SNDVG.

Enzyme and pathway databases

BioCycECOL439855:GHHB-436-MONOMER.
UniPathwayUPA00392.

Family and domain databases

Gene3D3.20.20.105. 1 hit.
HAMAPMF_00168. Q_tRNA_Tgt.
InterProIPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans-like.
[Graphical view]
PANTHERPTHR11962. PTHR11962. 1 hit.
PfamPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMSSF51713. SSF51713. 1 hit.
TIGRFAMsTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTGT_ECOSM
AccessionPrimary (citable) accession number: B1LJF4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 50 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

PATHWAY comments

Index of metabolic and biosynthesis pathways