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Protein

Queuine tRNA-ribosyltransferase

Gene

tgt

Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).UniRule annotation

Catalytic activityi

Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: tRNA-queuosine biosynthesis

This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway tRNA-queuosine biosynthesis and in tRNA modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei94Proton acceptorUniRule annotation1
Binding sitei148SubstrateUniRule annotation1
Binding sitei191SubstrateUniRule annotation1
Binding sitei218Substrate; via amide nitrogenUniRule annotation1
Active sitei268NucleophileUniRule annotation1
Metal bindingi306ZincUniRule annotation1
Metal bindingi308ZincUniRule annotation1
Metal bindingi311ZincUniRule annotation1
Metal bindingi337Zinc; via pros nitrogenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Queuosine biosynthesis, tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00392.

Names & Taxonomyi

Protein namesi
Recommended name:
Queuine tRNA-ribosyltransferaseUniRule annotation (EC:2.4.2.29UniRule annotation)
Alternative name(s):
Guanine insertion enzymeUniRule annotation
tRNA-guanine transglycosylaseUniRule annotation
Gene namesi
Name:tgtUniRule annotation
Ordered Locus Names:SAHV_1626
OrganismiStaphylococcus aureus (strain Mu3 / ATCC 700698)
Taxonomic identifieri418127 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000168611 – 379Queuine tRNA-ribosyltransferaseAdd BLAST379

Interactioni

Subunit structurei

Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA7X354.
SMRiA7X354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni94 – 98Substrate bindingUniRule annotation5
Regioni249 – 255RNA bindingUniRule annotation7
Regioni273 – 277RNA binding; important for wobble base 34 recognitionUniRule annotation5

Sequence similaritiesi

Belongs to the queuine tRNA-ribosyltransferase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000223473.
KOiK00773.
OMAiGIDLFDC.

Family and domain databases

Gene3Di3.20.20.105. 1 hit.
HAMAPiMF_00168. Q_tRNA_Tgt. 1 hit.
InterProiIPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans-like.
[Graphical view]
PfamiPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMiSSF51713. SSF51713. 1 hit.
TIGRFAMsiTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.

Sequencei

Sequence statusi: Complete.

A7X354-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAVTYEHIK TCKQSGARLG IVHTPHGSFE TPMFMPVGTK ATVKTMSPEE
60 70 80 90 100
LRQIEAKIIL GNTYHLWLQP GNDIIKHAGG LHKFMNWDGP ILTDSGGFQV
110 120 130 140 150
FSLSNLRKIT EEGVEFRHHT NGSKLFLSPE KSMQIQNDLG SDIMMAFDEC
160 170 180 190 200
PPMPAEYDYV KKSIERTTRW AKRCLDAHQR PEDQALFGII QGGEYEDLRE
210 220 230 240 250
QSAKDLVELD FPGYAIGGLS VGEPKPVMYK MVEHTEQFMP KDKPRYLMGV
260 270 280 290 300
GSPDALIECS IRGMDMFDCV LPTRIARNGT CMTSQGRLVI KNAKFADDLR
310 320 330 340 350
PLDENCDCYT CQNYSRAYIR HLIKAEETFG IRLTTIHNLH FLLKLMEDIR
360 370
QAIREDRLLD FKEEFFEQYG LNVENPKNF
Length:379
Mass (Da):43,310
Last modified:October 23, 2007 - v1
Checksum:i22E92081A3C147CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009324 Genomic DNA. Translation: BAF78509.1.
RefSeqiWP_001112045.1. NZ_CTYB01000003.1.

Genome annotation databases

EnsemblBacteriaiBAF78509; BAF78509; SAHV_1626.
GeneIDi28380773.
KEGGisaw:SAHV_1626.
PATRICi19558304. VBIStaAur127830_1670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009324 Genomic DNA. Translation: BAF78509.1.
RefSeqiWP_001112045.1. NZ_CTYB01000003.1.

3D structure databases

ProteinModelPortaliA7X354.
SMRiA7X354.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF78509; BAF78509; SAHV_1626.
GeneIDi28380773.
KEGGisaw:SAHV_1626.
PATRICi19558304. VBIStaAur127830_1670.

Phylogenomic databases

HOGENOMiHOG000223473.
KOiK00773.
OMAiGIDLFDC.

Enzyme and pathway databases

UniPathwayiUPA00392.

Family and domain databases

Gene3Di3.20.20.105. 1 hit.
HAMAPiMF_00168. Q_tRNA_Tgt. 1 hit.
InterProiIPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans-like.
[Graphical view]
PfamiPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMiSSF51713. SSF51713. 1 hit.
TIGRFAMsiTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTGT_STAA1
AccessioniPrimary (citable) accession number: A7X354
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: November 2, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.