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B5RQE7 (TGT_BORRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:BRE_820
OrganismBorrelia recurrentis (strain A1) [Complete proteome] [HAMAP]
Taxonomic identifier412418 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorrelia

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_1000097533

Sites

Active site901Nucleophile By similarity
Metal binding3051Zinc By similarity
Metal binding3071Zinc By similarity
Metal binding3101Zinc By similarity
Metal binding3361Zinc By similarity
Binding site911Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B5RQE7 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: D7EE88EE2F85C5B8

FASTA37542,950
        10         20         30         40         50         60 
MFNIIKNDKN SNARLGILEL PHGNVATPCF MPVGTLGVMK ALKHDVLEKL GCDLMLANTY 

        70         80         90        100        110        120 
HLYLRPGIDV IKKYGNLHNF TTWNKNFLTD SGGFQVFSLS NFRKIEDEGV DFKSHIDGSR 

       130        140        150        160        170        180 
HYFTPESVFS MQETFESDII MALDICSPYG IDYDEASLYT NITTSWARRT LCAYKNRKEG 

       190        200        210        220        230        240 
YEGLLFLITQ GNFFKDLRKR STELILELNS PGIAIGGISV GEPRDRYLEI LEYNSSLIPK 

       250        260        270        280        290        300 
DKPKYVMGIG TPHYILDAIY NGIDIFDCVN PTRIARHGSL LTDNGILRIN RAEFCFDTCS 

       310        320        330        340        350        360 
VERECSCTLC TRYSRGYLRH LFKSEEALGV MLASEHNIHY MFRLINKTKN AIMNDNFVKF 

       370 
RKLYLDKYDE GNLNE 

« Hide

References

[1]"The genome of Borrelia recurrentis, the agent of deadly louse-borne relapsing fever, is a degraded subset of tick-borne Borrelia duttonii."
Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.
PLoS Genet. 4:E1000185-E1000185(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000993 Genomic DNA. Translation: ACH95031.1.
RefSeqYP_002223252.1. NC_011244.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412418.BRE_820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH95031; ACH95031; BRE_820.
GeneID6919445.
KEGGbre:BRE_820.
PATRIC20570813. VBIBorRec40566_0825.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0343.
HOGENOMHOG000223473.
KOK00773.
OMAIVQGAFF.
OrthoDBEOG6SNDVG.

Enzyme and pathway databases

BioCycBREC412418:GJIA-820-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_BORRA
AccessionPrimary (citable) accession number: B5RQE7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 4, 2008
Last modified: May 14, 2014
This is version 45 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