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P28720 (TGT_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:ZMO0363
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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). 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.

Pathway

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

Subunit structure

Monomer.

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Sequence caution

The sequence AAA27704.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA27705.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG29862.1 differs from that shown. Reason: Erroneous initiation.

The sequence Z11910 differs from that shown. Reason: Frameshift at several positions.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 386385Queuine tRNA-ribosyltransferase HAMAP-Rule MF_00168
PRO_0000135563

Sites

Active site1021Nucleophile
Metal binding3181Zinc
Metal binding3201Zinc
Metal binding3231Zinc
Metal binding3491Zinc
Binding site1031Substrate

Experimental info

Mutagenesis1031S → A: Strongly reduces activity. Ref.6
Sequence conflict3121T → K Ref.1
Sequence conflict3121T → K Ref.2

Secondary structure

............................................................................ 386
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28720 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 26754E08600BD941

FASTA38642,843
        10         20         30         40         50         60 
MVEATAQETD RPRFSFSIAA REGKARTGTI EMKRGVIRTP AFMPVGTAAT VKALKPETVR 

        70         80         90        100        110        120 
ATGADIILGN TYHLMLRPGA ERIAKLGGLH SFMGWDRPIL TDSGGYQVMS LSSLTKQSEE 

       130        140        150        160        170        180 
GVTFKSHLDG SRHMLSPERS IEIQHLLGSD IVMAFDECTP YPATPSRAAS SMERSMRWAK 

       190        200        210        220        230        240 
RSRDAFDSRK EQAENAALFG IQQGSVFENL RQQSADALAE IGFDGYAVGG LAVGEGQDEM 

       250        260        270        280        290        300 
FRVLDFSVPM LPDDKPHYLM GVGKPDDIVG AVERGIDMFD CVLPTRSGRN GQAFTWDGPI 

       310        320        330        340        350        360 
NIRNARFSED LTPLDSECHC AVCQKWSRAY IHHLIRAGEI LGAMLMTEHN IAFYQQLMQK 

       370        380 
IRDSISEGRF SQFAQDFRAR YFARNS 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis and overexpression of the Zymomonas mobilis tgt gene encoding tRNA-guanine transglycosylase: purification and biochemical characterization of the enzyme."
Reuter K.K.H., Ficner R.
J. Bacteriol. 177:5284-5288(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, CHARACTERIZATION.
[2]"Sequence analysis of 44B6 fosmid clone of Zymomonas mobilis ZM4."
Ahn J.Y., Kang H.S.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.
[3]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.
[4]"Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis."
Shark K.B., Conway T.
FEMS Microbiol. Lett. 75:19-26(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.
[5]"Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange."
Romier C., Reuter K., Suck D., Ficner R.
EMBO J. 15:2850-2857(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[6]"Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity."
Graedler U., Ficner R., Garcia G.A., Stubbs M.T., Klebe G., Reuter K.
FEBS Lett. 454:142-146(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-382, MUTAGENESIS OF SER-103.
[7]"A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase."
Graedler U., Gerber H.-D., Goodenough-Lashua D.M., Garcia G.A., Ficner R., Reuter K., Stubbs M.T., Klebe G.
J. Mol. Biol. 306:455-467(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[8]"De novo design, synthesis, and in vitro evaluation of inhibitors for prokaryotic tRNA-guanine transglycosylase: a dramatic sulfur effect on binding affinity."
Meyer E.A., Brenk R., Castellano R.K., Furler M., Klebe G., Diederich F.
ChemBioChem 3:250-253(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-386.
[9]"Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysis."
Brenk R., Naerum L., Graedler U., Gerber H.-D., Garcia G.A., Reuter K., Stubbs M.T., Klebe G.
J. Med. Chem. 46:1133-1143(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-386.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33777 Genomic DNA. Translation: AAA27704.1. Different initiation.
L33777 Genomic DNA. Translation: AAA27705.1. Different initiation.
AF313764 Genomic DNA. Translation: AAG29862.1. Different initiation.
AE008692 Genomic DNA. Translation: AAV88987.2.
Z11910 Genomic DNA. No translation available.
PIRT46898.
RefSeqYP_162098.2. NC_006526.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFZX-ray2.00A1-386[»]
1ENUX-ray1.95A1-386[»]
1F3EX-ray1.85A1-386[»]
1K4GX-ray1.70A1-386[»]
1K4HX-ray1.80A1-386[»]
1N2VX-ray2.10A1-386[»]
1OZMX-ray1.95A2-385[»]
1OZQX-ray1.90A2-385[»]
1P0BX-ray1.70A2-385[»]
1P0DX-ray1.90A2-385[»]
1P0EX-ray2.40A2-385[»]
1PUDX-ray1.85A1-386[»]
1PXGX-ray1.70A2-382[»]
1Q2RX-ray2.90A/B/C/D2-385[»]
1Q2SX-ray3.20A/B/C/D2-385[»]
1Q4WX-ray1.93A1-386[»]
1Q63X-ray1.85A1-386[»]
1Q65X-ray2.10A1-386[»]
1Q66X-ray1.75A1-386[»]
1R5YX-ray1.20A2-385[»]
1S38X-ray1.81A1-386[»]
1S39X-ray1.95A1-386[»]
1WKDX-ray2.60A2-385[»]
1WKEX-ray2.20A2-385[»]
1WKFX-ray2.20A2-385[»]
1Y5VX-ray1.58A2-385[»]
1Y5WX-ray1.58A2-385[»]
1Y5XX-ray2.10A/D2-385[»]
2BBFX-ray1.70A1-386[»]
2NQZX-ray1.46A2-386[»]
2NSOX-ray1.60A1-386[»]
2OKOX-ray1.50A2-386[»]
2POTX-ray1.80A1-386[»]
2PWUX-ray1.77A1-386[»]
2PWVX-ray1.70A1-386[»]
2QIIX-ray1.70A1-386[»]
2QZRX-ray1.95A2-386[»]
2Z1VX-ray1.55A1-386[»]
2Z1WX-ray1.63A1-386[»]
2Z1XX-ray1.63A1-386[»]
2Z7KX-ray1.28A1-386[»]
3BL3X-ray2.25A1-386[»]
3BLDX-ray1.19A1-386[»]
3BLLX-ray1.26A1-386[»]
3BLOX-ray1.60A1-386[»]
3C2NX-ray1.58A1-386[»]
3C2YX-ray1.78A1-386[»]
3C2ZX-ray1.65A1-386[»]
3EOSX-ray1.78A1-386[»]
3EOUX-ray1.93A1-386[»]
3GC4X-ray1.80A1-386[»]
3GC5X-ray1.40A1-386[»]
3GE7X-ray1.50A1-386[»]
3GEVX-ray1.53A1-386[»]
3HFYX-ray2.00A1-386[»]
3RR4X-ray1.68A1-386[»]
3S1GX-ray1.82A1-386[»]
3SM0X-ray1.57A1-386[»]
3TLLX-ray1.37A1-386[»]
3UNTX-ray1.80A1-386[»]
3UVIX-ray1.55A1-386[»]
3V0YX-ray1.64A1-386[»]
4DXXX-ray1.66A1-386[»]
4DY1X-ray2.04A1-386[»]
4E2VX-ray1.18A1-386[»]
4FPSX-ray1.45A1-386[»]
4FR1X-ray1.74A1-386[»]
4FR6X-ray1.59A1-386[»]
4FSAX-ray1.62A1-386[»]
4GCXX-ray1.42A1-386[»]
4GD0X-ray1.29A1-386[»]
4GG9X-ray1.48A1-386[»]
4GH1X-ray1.45A1-386[»]
4GH3X-ray2.06A1-386[»]
4GHRX-ray2.00A1-386[»]
4GI4X-ray1.97A1-386[»]
4GIYX-ray1.75A1-386[»]
4GKTX-ray1.53A1-386[»]
4H6EX-ray1.42A1-386[»]
4H7ZX-ray1.68A1-386[»]
4HQVX-ray1.66A2-386[»]
4HSHX-ray1.56A2-386[»]
4HTBX-ray1.90A1-386[»]
4HVXX-ray1.82A1-386[»]
4IPPX-ray1.33A1-386[»]
ProteinModelPortalP28720.
SMRP28720. Positions 11-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO0363.

Chemistry

BindingDBP28720.
ChEMBLCHEMBL2987.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV88987; AAV88987; ZMO0363.
GeneID3188564.
KEGGzmo:ZMO0363.
PATRIC32566062. VBIZymMob102260_0345.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0343.
HOGENOMHOG000223473.
KOK00773.
ProtClustDBPRK00112.

Enzyme and pathway databases

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...

Other

EvolutionaryTraceP28720.

Entry information

Entry nameTGT_ZYMMO
AccessionPrimary (citable) accession number: P28720
Secondary accession number(s): Q5NQL7, Q60247, Q9F5L7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 125 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways