Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5P720 (TGT_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 63. 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
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:AZOSEA07680
ORF Names:ebA1415
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum ›

Protein attributes

Sequence length370 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.

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: HAMAP

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

queuine tRNA-ribosyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Queuine tRNA-ribosyltransferase HAMAP-Rule MF_00168
PRO_0000135443

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
Q5P720 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: E8679EE1AFB16B91

FASTA37040,455
        10         20         30         40         50         60 
MQFELLAQHG AARRGRLTLA HGTVDTPAFM PVGTYGTVKA MTPAALADTG AQICLGNTFH 

        70         80         90        100        110        120 
LWLRPGLDVV AAHGGLHRFM NWDRPILTDS GGFQVFSLGA LRKISEEGVK FASPIDGAKL 

       130        140        150        160        170        180 
FLTPEESMRI QTVLNSDIAM IFDECTPHPA THDEAAKSMQ LSLRWARRSR DEFDRLANPN 

       190        200        210        220        230        240 
ALFGIVQGGM FEDLRDESLA ALDAIGFSGY AIGGLSVGEP KEDMARILAH TAPRLPAGRP 

       250        260        270        280        290        300 
RYLMGVGTPE DIVAGVAAGI DMFDCVMPTR NARNGWLFTR YGDIKIKNAT HKQDTRPLDP 

       310        320        330        340        350        360 
SCDCYTCRNF SRAYLHHLHR AGEILGSMLN TIHNLRYYQT LTAELRAAIA AGDLDSHAAR 

       370 
FRADRSTGAC

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR555306 Genomic DNA. Translation: CAI06891.1.
RefSeqYP_157792.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5P720.
SMRQ5P720. Positions 1-363.
ModBaseSearch...

Protein-protein interaction databases

STRING76114.ebA1415.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI06891; CAI06891; ebA1415.
GeneID3182932.
KEGGeba:ebA1415.
PATRIC20967633. VBIAroAro98752_0777.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0343.
HOGENOMHOG000223473.
KOK00773.
OMAMSPERSI.
ProtClustDBPRK00112.

Enzyme and pathway databases

BioCycAARO76114:GJTA-787-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.
[Graphical view]
PANTHERPTHR11962. PTHR11962. 1 hit.
PfamPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMSSF51713. tRNA_ribo_trans. 1 hit.
TIGRFAMsTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTGT_AROAE
AccessionPrimary (citable) accession number: Q5P720
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 4, 2005
Last modified: May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents