Tgt

• Description: tRNA-guanine transglycosylase
  
  

Gene name	tgt
Synonyms
Essential	no
Product	tRNA-guanine transglycosylase
Function	tRNA modification
Gene expression levels in SubtiExpress: tgt
MW, pI	43 kDa, 6.149
Gene length, protein length	1143 bp, 381 aa
Immediate neighbours	yrbF, queA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation, membrane proteins

The gene

Basic information

• Locus tag: BSU27710

Database entries

• BsubCyc: BSU27710

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: [tRNA]-guanine + queuine = [tRNA]-queuine + guanine (according to Swiss-Prot)

• Protein family: queuine tRNA-ribosyltransferase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• BsubCyc: BSU27710

• Structure:

• UniProt: O32053

• KEGG entry: [2]

• E.C. number: 2.4.2.29

Expression and regulation

• Operon:

• Expression browser: tgt PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 258 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 1005 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Ruth Brenk, Milton T Stubbs, Andreas Heine, Klaus Reuter, Gerhard Klebe
Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase and their implications for substrate selectivity, reaction mechanism and structure-based drug design.
Chembiochem: 2003, 4(10);1066-77
[PubMed:14523925] [WorldCat.org] [DOI] (P p)

Wei Xie, Xianjun Liu, Raven H Huang
Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate.
Nat Struct Biol: 2003, 10(10);781-8
[PubMed:12949492] [WorldCat.org] [DOI] (P p)

DeeAnne M Goodenough-Lashua, George A Garcia
tRNA-guanine transglycosylase from E. coli: a ping-pong kinetic mechanism is consistent with nucleophilic catalysis.
Bioorg Chem: 2003, 31(4);331-44
[PubMed:12877882] [WorldCat.org] [DOI] (P p)

G A Garcia, D L Tierney, S Chong, K Clark, J E Penner-Hahn
X-ray absorption spectroscopy of the zinc site in tRNA-guanine transglycosylase from Escherichia coli.
Biochemistry: 1996, 35(9);3133-9
[PubMed:8608154] [WorldCat.org] [DOI] (P p)

A W Curnow, G A Garcia
tRNA-guanine transglycosylase from Escherichia coli. Minimal tRNA structure and sequence requirements for recognition.
J Biol Chem: 1995, 270(29);17264-7
[PubMed:7615526] [WorldCat.org] [DOI] (P p)

S Chong, A W Curnow, T J Huston, G A Garcia
tRNA-guanine transglycosylase from Escherichia coli is a zinc metalloprotein. Site-directed mutagenesis studies to identify the zinc ligands.
Biochemistry: 1995, 34(11);3694-701
[PubMed:7893665] [WorldCat.org] [DOI] (P p)

S O Mueller, R K Slany
Structural analysis of the interaction of the tRNA modifying enzymes Tgt and QueA with a substrate tRNA.
FEBS Lett: 1995, 361(2-3);259-64
[PubMed:7698334] [WorldCat.org] [DOI] (P p)

A W Curnow, F L Kung, K A Koch, G A Garcia
tRNA-guanine transglycosylase from Escherichia coli: gross tRNA structural requirements for recognition.
Biochemistry: 1993, 32(19);5239-46
[PubMed:8494901] [WorldCat.org] [DOI] (P p)

S Noguchi, Y Nishimura, Y Hirota, S Nishimura
Isolation and characterization of an Escherichia coli mutant lacking tRNA-guanine transglycosylase. Function and biosynthesis of queuosine in tRNA.
J Biol Chem: 1982, 257(11);6544-50
[PubMed:6804468] [WorldCat.org] (P p)